DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Claims
Claims 1-25 are pending.
Claims 1-25 are examined herein.
Claims 1-25 are rejected.
Priority
Application No. 18/709,433 filed on 05/10/2024 is a 371 of PCT Application No. PCT/EP2022/081497 filed on 11/10/2022 and also claims foreign priority to GB2116307.6 filed on 11/12/2021.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Election/Restrictions
Inventios I and III-IV, encompassing claims 1-18 and 22-25, are rejoined and examined herein. Because a claimed invention previously withdrawn from consideration has been rejoined, the restriction requirement between groups I-IV as set forth in the Office action mailed on 04/22/2026 is hereby withdrawn. In view of the withdrawal of the restriction requirement as to the rejoined inventions, applicant(s) are advised that if any claim presented in a divisional application is anticipated by, or includes all the limitations of, a claim that is allowable in the present application, such claim may be subject to provisional statutory and/or nonstatutory double patenting rejections over the claims of the instant application.
Once the restriction requirement is withdrawn, the provisions of 35 U.S.C. 121 are no longer applicable. See In re Ziegler, 443 F.2d 1211, 1215, 170 USPQ 129, 131-32 (CCPA 1971). See also MPEP § 804.01.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
This application contains sequence disclosures in accordance with the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.831(a) and 1.831(b). However, this application fails to comply with the requirements of 37 CFR 1.831-1.834. The examiner has noted that claims 1 and 4 reference SEQ ID NOs: 1-6, of which the sequences have not been provided in XML. Applicant must provide:
• A replacement “Sequence Listing XML” part of the disclosure, as described above in item 1. or 2., as well as
• A statement that identifies the location of all additions, deletions, or replacements of sequence information in the “Sequence Listing XML” as required by 1.835(b)(3);
• A statement that indicates support for the amendment in the application, as filed, as required by 37 CFR 1.835(b)(4);
• A statement that the “Sequence Listing XML” includes no new matter in accordance with 1.835(b)(5); and
• A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation by reference paragraph as required by 37 CFR 1.835(b)(2), consisting of:
o A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
o A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Claim Rejections - 35 USC § 112
Indefiniteness
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-25 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites “SEQ ID NO:1”. Additionally, claim 4 recites “SEQ ID NO: 2”, “SEQ ID NO: 3”, “SEQ ID NO: 4”, “SEQ ID NO: 5”, and “SEQ ID NO: 6”. These sequence identifiers appear to represent the amino acid sequence of F[V/M]TX[F/Y], or variations of the motif. However, because the sequences of the sequence identifiers are not provided in the sequence listing, it is unclear what the sequence identifiers represent. For this reason, the claims are indefinite.
Claims 2-3 and 5-25 are rejected as a function of dependency.
Claim 12 recites the limitation "the HST-inhibiting herbicide". However, there is no previous recitation of an HST-inhibiting herbicide in claim 12 or claim 1 (from which claim 12 depends). It is unclear what the recitation is in reference to, and therefore there is insufficient antecedent basis for this limitation in the claim.
Claim 17 recites the limitation "the nucleic acid or the expression vector". However, there is no previous recitation of the nucleic acid or the expression vector in claim 17 or claims 1 and 16 (from which claim 17 depends). It is unclear what the recitation is in reference to, and therefore there is insufficient antecedent basis for this limitation in the claim.
Claim 22 recites the limitation "…comprising the expression in the plant, part or cell of an HST enzyme according to claim 1". However, there is no previous recitation of expression in the plant, part or cell of an HST enzyme in claim 22 or claim 1 (from which claim 22 depends). It is unclear what the recitation of “the expression” is in reference to, and therefore there is insufficient antecedent basis for this limitation in the claim. Furthermore, Applicant may consider amending claim 22 to read “…comprising expressing the HST enzyme according to claim 1 in the plant, plant part, or cell.” To improve clarity of the claim.
Claim 24 recites the limitation "the plant, plant part, plant cell or protoplast". However, there is no previous recitation of a protoplast in claim 24 or claims 1 and 13 (from which claim 24 depends). It is unclear what the recitation is in reference to, and therefore there is insufficient antecedent basis for this limitation in the claim.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claims 2, 3, 7, 9, 15, and 21 recite a broad recitation, and the claim also recites “preferably,…” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-4, 6-7, 9, 12, and 16-18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Uniprot Accession No. A0A061SAB2 (Uniprot Accession No. A0A061SAB2, Homogentisate solanesyltransferase, published online 09/03/2014.).
Regarding claim 1, Uniprot Accession No. A0A061SAB2 discloses a Homogentisate solanesyltransferase (HST) enzyme comprising the amino acid motif FATIF, wherein I represents the X in instant SEQ ID NO: 1 and A is the amino acid residue of SEQ ID NO: 1 that is mutated.
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Regarding claim 2, Uniprot Accession No. A0A061SAB2 discloses a Homogentisate solanesyltransferase (HST) enzyme comprising the amino acid motif FATIF, therefore X (i.e. position 4) is an isoleucine.
Regarding claim 3, Uniprot Accession No. A0A061SAB2 discloses position 2 is an alanine which is an aliphatic amino acid in substitution of V or M in instant SEQ ID NO: 1.
Regarding claim 4, Uniprot Accession No. A0A061SAB2 discloses position 2 is an alanine in substitution of V or M in instant SEQ ID NO: 1.
Regarding claim 9, Uniprot Accession No. A0A061SAB2 discloses a sequence on either side of FATIF (i.e. wherein the HST enzyme comprises an additional amino acid sequence).
Regarding claim 13, Uniprot Accession No. A0A061SAB2 discloses the protein sequence of the HST enzyme was determined from the transcriptome of the halophilic microalga Tetraselmis sp. GSL018, and therefore discloses a nucleic acid that has been isolated (evidenced by its sequencing) comprising a nucleotide sequence encoding a HST enzyme as set forth in instant claim 1.
Regarding claim 16, Uniprot Accession No. A0A061SAB2 discloses the sequences is derived from Tetraselmis (i.e. an algae/ plant cell).
Regarding claim 17, because Uniprot Accession No. A0A061SAB2 discloses the protein sequence of the HST enzyme was determined from the transcriptome of the halophilic microalga Tetraselmis sp. GSL018, the protein must have been expressed from the nucleic acid in the algae/ plant cell.
Regarding claim 22, Uniprot Accession No. A0A061SAB2 discloses the protein sequence of the HST enzyme was determined from the transcriptome of the halophilic microalga Tetraselmis sp. GSL018, therefore the protein of the HST enzyme that satisfies the limitations of claim 1 must have been expressed in the algae/ plant cell. Because the method merely requires expression in a plant, part or cell of an HST enzyme according to claim 1, the method of claim 22 is therefore also disclosed by Uniprot Accession No. A0A061SAB2.
Claims 6, 7, 12, and 18 are also anticipated as a function of inherency. The claims require wherein the HST enzyme is at least partially resistant to inhibition by an HST-inhibiting compound (claim 6), wherein the HST enzyme is at least 10-fold more resistant to inhibition by an HST-inhibiting compound than a control HST enzyme not having the mutation (claim 7), wherein the HST-inhibiting herbicide is selected from one or more of: compound B5a, compound B5b, compound B5u, and compound B8a (claim 12), and wherein the plant cell has an increased resistance to an HST-inhibiting herbicide as compared to a corresponding control plant cell (claim 18). The instant specification teaches an algae species (C. fusca) with an alanine (A) amino acid at position 2 of SEQ ID NO: 1 in an HST sequence has increased resistance to B5u, B5p, and B5m as compared to when position 2 of SEQ ID NO: 1 in an HST sequence is a valine (V) (see p. 80, Table 2, and p. 81, Tables 4-5). The instant specification also teaches tobacco plants with an alanine (A) amino acid at position 2 of SEQ ID NO: 1 in an HST sequence has increased resistance to B5u, B5a, B5b, and B8a as compared to when position 2 of SEQ ID NO: 1 in an HST sequence is a valine (V) (see p. 87, Table 11, and p. 93, Table 20). Since Uniprot Accession No. A0A061SAB2 also comprises an alanine (A) amino acid at position 2 of SEQ ID NO: 1 in an HST sequence, the HST enzyme would inherently be at least partially resistant to inhibition by an HST-inhibiting compound (as required by claim 6). Similarly, the specification evidences the C. fusca HST enzyme with alanine at position 2 of SEQ ID NO: 1 in an HST sequence is at least 16-fold more resistant to inhibition by an HST-inhibiting compound than a control HST (comprising the Valine), and because Uniprot Accession No. A0A061SAB2 also comprises an alanine (A) amino acid at position 2 of SEQ ID NO: 1 in an HST sequence, the HST enzyme would inherently also be at least 10-fold more resistant to inhibition by an HST-inhibiting compound than a control HST enzyme not having the mutation (i.e. wherein the enzyme comprises the valine). Claim 12 is interpreted to have meant the HST enzyme of claim 1 is more resistant to inhibition by one of the listed herbicides, and as described immediately above the alanine at position 2 in several HST enzymes confers increased resistance to inhibition by the listed herbicides. Furthermore, because the instant specification evidences C. fusca and N. tabacum plants comprising either a C. fusca, O. sativa, or A. thaliana HST enzyme with A at position 2 of instant SEQ ID NO: 1 increased resistance of the plant/ plant cell to several HST-inhibiting herbicides, and because Uniprot Accession No. A0A061SAB2 discloses the Tetraselmis algae comprises an A at position 2 of SEQ ID NO: 1 in the Tetraselmis HST enzyme, the Tetraselmis plant/ plant cell comprising the HST enzyme of Uniprot Accession No. A0A061SAB2 would be expected to inherently have increased resistance to an HST-inhibiting herbicide as compared to a control plant (i.e. the control plant being wherein the HST enzyme does not have an A at position 2 of SEQ ID NO: 1, and e.g. wherein the enzyme comprises a valine at position 2 of SEQ ID NO: 1).
Claims 1, 3, 5, 9-10, 13, 16-17, and 22 are separately rejected under 35 U.S.C. 102(a)(1) as being anticipated by Uniprot Accession No. A0A6D2HSL1 (Uniprot Accession No. A0A6D2HSL1, published online 04/07/2021.).
Regarding claim 1, Uniprot Accession No. A0A6D2HSL1 discloses a Homogentisate solanesyltransferase (HST) enzyme comprising the amino acid motif FVKLF, wherein L represents the X in instant SEQ ID NO: 1 and K is the amino acid residue of SEQ ID NO: 1 that is mutated.
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Regarding claim 3, Uniprot Accession No. A0A6D2HSL1 discloses position 3 is a lysine which is a substitution of T in instant SEQ ID NO: 1.
Regarding claim 5, Uniprot Accession No. A0A6D2HSL1 discloses the motif is comprised within an amino acid sequence that has 76.1% identity (i.e. at least 70% identity) to instant SEQ ID NO: 16 (see alignment below).
Regarding claim 9, Uniprot Accession No. A0A6D2HSL1 discloses a sequence on either side of FVKLF (i.e. wherein the HST enzyme comprises an additional amino acid sequence).
Regarding claim 10, Uniprot Accession No. A0A6D2HSL1 has over 74% sequence identity to instant SEQ ID NO: 29 (see alignment below).
Regarding claim 13, Uniprot Accession No. A0A6D2HSL1 discloses the amino acid sequence of the HST enzyme comprises a sequenced nucleotide that encodes the protein, and therefore discloses a nucleic acid that has been isolated (evidenced by its sequencing) comprising a nucleotide sequence encoding a HST enzyme as set forth in instant claim 1.
Regarding claim 16, Uniprot Accession No. A0A6D2HSL1 discloses the sequences is derived from Microthlaspi erraticum (i.e. a plant).
Regarding claim 17, Uniprot Accession No. A0A6D2HSL1 discloses the sequences is derived from Microthlaspi erraticum (i.e. a plant). The sequence is reasonably interpreted to be expressed in the plant since it is closely tied to chloroplast function and photosynthesis, and therefore is reasonably interpreted to satisfy the claim limitation of wherein the HST enzyme is actively expressed from the nucleic acid.
Regarding claim 22, Uniprot Accession No. A0A6D2HSL1 discloses the protein sequence of the HST enzyme. This protein is reasonably interpreted to be expressed in the plant (see claim 17 rejection). Because the method merely requires expression in a plant, part or cell of an HST enzyme according to claim 1, the method of claim 22 is therefore also disclosed by Uniprot Accession No. A0A6D2HSL1.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 14-15, 19-21, and 23-24 are rejected under 35 U.S.C. 103 as being unpatentable over Uniprot Accession No. A0A6D2HSL1 (Uniprot Accession No. A0A6D2HSL1, published online 04/07/2021.) as applied to claims 1 and 13 above, and further in view of Pasternak (US-10829778-B2).
Regarding claims 15-15, 19-21, and 23-24, Uniprot Accession No. A0A6D2HSL1 teaches the limitations of claims 1 and 13 as set forth in the previous anticipation rejection. The teachings of Uniprot Accession No. A0A6D2HSL1 as they are applied to claim 1 are set forth previously herein and are incorporated by reference.
However, Uniprot Accession No. A0A6D2HSL1 does not explicitly teach a an expression vector comprising a nucleic acid of claim 13 (claim 14), an expression vector as claimed in claim 14, further comprising an expression regulatory sequence or sequences (claim 15), a method of controlling undesired vegetation in the vicinity of a plant according to any of claim 16, the method comprising applying an effective amount of at least one HST-inhibiting herbicide to the undesired vegetation and to said plant (claim 19), a method of enhancing growth of a plant of any of claim 16 by controlling undesired vegetation in the vicinity of the plant, the method comprising applying an effective amount of at least one HST-inhibiting herbicide to the undesired vegetation and to the plant (claim 20), wherein the effective amount of said HST-inhibiting herbicide does not substantially inhibit the growth of the plant (claim 21), transforming a plant with the nucleic acid molecule (claim 24), nor crossing a first plant comprising the nucleic acid molecule of claim 13 with a second plant and obtaining seeds (claim 23).
In analogous art, Pasternak teaches a method for controlling undesired vegetation at a plant cultivation site, the method comprising the steps of providing a plant that comprises a nucleic acid comprising a nucleotide sequence encoding a wildtype homogentisate solanesyl transferase or a mutated homogentisate solanesyl transferase (mut-HST) which is resistant or tolerant to a N-heterocyclyl-arylcarboxamide b) applying to said site an effective amount of said herbicide (Col. 3, lines 9-24). Pasternak further teaches expression vectors for overexpressing the HST enzyme in transgenic soybean plants (Fig. 2), which comprises an expression regulatory sequence (i.e. a PcUbi promoter). Pasternak teaches an effective amount is intended to mean an amount and concentration that is sufficient to kill or inhibit the growth of a similar, wild-type, plant, plant tissue, plant cell, or host cell, but that said amount does not kill or inhibit as severely the growth of the herbicide-resistant plants, plant tissues, plant cells, and host cells of the present invention (Col. 12, lines 1-12). Pasternak also teaches the term “control of undesired vegetation” is to be understood as meaning the killing of weeds and/or otherwise retarding or inhibiting the normal growth of the weeds, and therefore the herbicide is interpreted to also be applied to the undesired vegetation in an effective amount (col. 8, lines 47-49). Pasternak teaches expressing of the nucleic acid encoding HST or mut-HST in the plant results in the plants increased resistance to N-heterocyclyl-arylcarboxamide, thus N-heterocyclyl-arylcarboxamide is interpreted as an HST-inhibiting herbicide (col. 77, lines 10-13). Furthermore, Pasternak teaches The N-heterocyclyl-arylcarboxamides useful for the present invention are often best applied in conjunction with one or more other HPPD- and/or HST targeting herbicides to obtain control of a wider variety of undesirable vegetation (Col. 22, lines 16-25). Pasternak further teaches crossing a first plant that is a herbicide-resistant plant of the invention to a second plant that may or may not be resistant to the same herbicide or herbicides as the first plant or may be resistant to different herbicide or herbicides than the first plant, wherein the second plant can be any plant that is capable of producing viable progeny plants (i.e., seeds) when crossed with the first plant, and selecting progeny that comprise the mut-HST polypeptides (Col. 80, lines 32-51).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention of as taught by Pasternak to include the HST amino acid sequence taught by Uniprot Accession No. A0A6D2HSL1 to arrive at the instantly claimed method with a reasonable expectation of success because the HST amino acid sequence taught by Uniprot Accession No. A0A6D2HSL1 was a known and readily obtainable sequence and cloning of expression vectors is routine in the art. One having ordinary skill in the art would have been motivated to combine the teachings because it would have been prima facie obvious to substitute the HST amino acid sequence taught by Pasternak with another HST amino acid sequence known in the art, Uniprot Accession No. A0A6D2HSL1, for the same purpose. By doing so, the ordinary artisan would arrive at the claimed expression vector and a plant comprising it. One of ordinary skill in the art would have also been motivated to combine the teachings and arrive at the instantly claimed vectors, plants, and methods for the purpose of increasing resistance to the N-heterocyclyl-arylcarboxamide herbicide as taught by Pasternak. Furthermore, the ordinary artisan would have been motivated to cross the plants of Pasternak expressing the alternative HST polypeptide with a second plant and obtain progeny for the purpose of obtaining progeny comprising the HST polypeptide that confers increased herbicide resistance as taught by Pasternak (Col. 80, lines 32-51), as well as apply the HST-inhibiting herbicide to the plant and undesired vegetation for the purpose of controlling the undesired vegetation as taught by Pasternak (Col. 3, lines 9-24).
Alignments:
Alignment of instant SEQ ID NO: 16 (Qy) with Uniprot Accession No. A0A6D2HSL1 (Db):
RESULT 41
A0A6D2HSL1_9BRAS
ID A0A6D2HSL1_9BRAS Unreviewed; 360 AA.
AC A0A6D2HSL1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Homogentisate phytyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MERR_LOCUS3409 {ECO:0000313|EMBL:CAA7016174.1};
OS Microthlaspi erraticum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Coluteocarpeae; Microthlaspi.
OX NCBI_TaxID=1685480 {ECO:0000313|EMBL:CAA7016174.1, ECO:0000313|Proteomes:UP000467841};
RN [1] {ECO:0000313|EMBL:CAA7016174.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mishra B.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000256|ARBA:ARBA00004508}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004508}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005985}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAA7016174.1}.
CC ---------------------------------------------------------------------------
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DR EMBL; CACVBM020000222; CAA7016174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6D2HSL1; -.
DR OrthoDB; 1502398at2759; -.
DR Proteomes; UP000467841; Unassembled WGS sequence.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:InterPro.
DR CDD; cd13960; PT_UbiA_HPT1; 1.
DR Gene3D; 1.10.357.140; UbiA prenyltransferase; 1.
DR InterPro; IPR044502; AtHST-like.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR43009; HOMOGENTISATE SOLANESYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43009:SF10; HOMOGENTISATE SOLANESYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000467841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 360 AA; 39997 MW; 3E88B4EB2569A54A CRC64;
Query Match 76.1%; Score 1491; Length 360;
Best Local Similarity 78.4%;
Matches 312; Conservative 6; Mismatches 28; Indels 52; Gaps 5;
Qy 1 MELSISQSPRVRFSSLAPRFLAASHHHRPSVHLAGKFISLPRDVRFTSLSTSRMRSKFVS 60
|| |||||||:||| |||| ||| || |||||||| | || | ||||||||||||
Db 1 MEFSISQSPRLRFS---PRFLVASH---PSSHLAGKFISRPIDVASTGLSTSRMRSKFVS 54
Qy 61 TNYRKISIR-------------ACSQVGAAESDDPVLDRIARFQNACWRFLRPHTIRGTA 107
||||||||| ||||| | | || ||::| ||| |||||||||| |||
Db 55 TNYRKISIRALFNGTHKRRYYQACSQVDAPGS-DPFLDKVAHFQNTCWRFLRPHTIHGTA 113
Qy 108 LGSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLP 167
||||||| |||| |||||| ||||||||||||:|||||||||||||||||||||||||||
Db 114 LGSTALVARALIGNTHLIKRSLVLKALSGLLAVICGNGYIVGINQIYDIGIDKVNKPYLP 173
Qy 168 IAAGDLSVQSAWLLVIFFAIA GLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPV 227
||||||||:||||||||||||||| | ||||||| ||||||||||||| |||||||
Db 174 IAAGDLSVRSAWLLVIFFAIA GLLNALHAFDPFITSLYCLGLFLGTIYSVPPFRMKRFPV 233
Qy 228 AAFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFVTLFALVIAITKDLPDVE 287
||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||||
Db 234 AAFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFVKLFALVIAITKDLPDVE 293
Qy 288 GDRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFRGSLMIPAHVILASG 347
|||||||||||||||||||||||||||||||:|||||||||||
Db 294 GDRKFQISTLATKLGVRNIAFLGSGLLLVNYISAISLAFYMPQ----------------- 336
Qy 348 LIFQTWVLEKANYTKEAISGYYRFIWNLFYAEYLLFPF 385
||| |||||||||||||||||||
Db 337 ---------------EAIGGYYRFIWNLFYAEYLLFPF 359
Alignment of Uniprot Accession No. A0A6D2HSL1 (Query) with instant SEQ ID NO: 29 (Sbjct):
Alignment statistics for match #1
Score
Expect
Identities
Positives
Gaps
543 bits(1399)
0.0
294/397(74%)
308/397(77%)
43/397(10%)
Query 1 MEFSISQSPRLRFS---PRFLVASH---PSSHLAGKFISRPIDVASTGLSTSRMRSKFVS 54
ME SISQSPR+RFS PRFL ASH PS HLAGKFIS P DV T LSTSRMR V+
Sbjct 1 MELSISQSPRVRFSSLAPRFLAASHHHRPSVHLAGKFISLPRDVRFTSLSTSRMRILAVA 60
Query 55 TNYRKISIRALFNGTHKRRYYQACSQVDAPGSDPFLDKVAHFQNTCWRFLRPHTIHGTAL 114
++ + + K + ++ D DP LD++A FQN CWRFLRPHTI GTAL
Sbjct 61 LTFKSRCVYVNYE-IPKDQILVGAAESD----DPVLDRIARFQNACWRFLRPHTIRGTAL 115
Query 115 GSTALVARALIGNTHLIKRSLVLKALSGLLAVICGNGYIVGINQIYDIGIDKVNKPYLPI 174
GSTALV RALI NTHLIK SLVLKALSGLLA+ICGNGYIVGINQIYDIGIDKVNKPYLPI
Sbjct 116 GSTALVTRALIENTHLIKWSLVLKALSGLLALICGNGYIVGINQIYDIGIDKVNKPYLPI 175
Query 175 AAGDLSVRSAWLLVIFFAIA GLLNALHAFDPFITSLYCLGLFLGTIYSVPPFRMKRFPVA 234
AAGDLSV+SAWLLVIFFAIA GLL F PFITSLY LGLFLGTIYSVPP RMKRFPVA
Sbjct 176 AAGDLSVQSAWLLVIFFAIA GLLVVGFNFGPFITSLYSLGLFLGTIYSVPPLRMKRFPVA 235
Query 235 AFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFVKLFALVIAITKDLPDVEG 294
AFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFV LFALVIAITKDLPDVEG
Sbjct 236 AFLIIATVRGFLLNFGVYHATRAALGLPFQWSAPVAFITSFVNLFALVIAITKDLPDVEG 295
Query 295 DRKFQISTLATKLGVRNIAFLGSGLLLVNYISAISLAFYMPQ------------------ 336
DRKFQISTLATKLGVRNIAFLGSGLLLVNY+SAISLAFYMPQ
Sbjct 296 DRKFQISTLATKLGVRNIAFLGSGLLLVNYVSAISLAFYMPQVFRGSLMIPAHVILASGL 355
Query 337 --------------EAIGGYYRFIWNLFYAEYLLFPF 359
EAI GYYRFIWNLFYAEYLLFPF
Sbjct 356 IFQTWVLEKANYTKEAISGYYRFIWNLFYAEYLLFPF 392
Closest Prior Art
Claims 8, 11, and 25 appear free of the prior art.
Regarding claims 8, 11, and 25, the closest prior art is Pasternak (US-10829778-B2). Pasternak teaches a method for controlling undesired vegetation at a plant cultivation site, the method comprising the steps of providing a plant that comprises a nucleic acid comprising a nucleotide sequence encoding a wildtype homogentisate solanesyl transferase or a mutated homogentisate solanesyl transferase (mut-HST) which is resistant or tolerant to a N-heterocyclyl-arylcarboxamide b) applying to said site an effective amount of said herbicide (Col. 3, lines 9-24). Pasternak further teaches expression vectors for overexpressing the HST enzyme in transgenic soybean plants (Fig. 2). However, Pasternak does not teach, suggest, or otherwise render obvious mutating the WT HST sequences in the motif region of F[V/M]TX[F/Y] to arrive at the instantly claimed mutant sequences in claims 8 and 11. The claimed sequences do not expressly appear in the prior art. Additionally, because Pasternak does not teach, suggest, or otherwise render obvious mutating the WT HST sequences in the motif of F[V/M]TX[F/Y], Pasternak also does not teach, suggest, or otherwise render obvious editing the endogenous nucleic acid sequence of the plant encoding an HST enzyme to produce nucleic acid sequence of claim 13 which comprises mutations in the F[V/M]TX[F/Y] motif.
Conclusion and Inquiries
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JESSICA N STOCKDALE whose telephone number is (703)756-5395. The examiner can normally be reached M-F 8:30-5:00 CT.
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JESSICA N. STOCKDALE
Examiner
Art Unit 1663
/JESSICA NICOLE STOCKDALE/Examiner, Art Unit 1663
/CHARLES LOGSDON/Primary Examiner, Art Unit 1662
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