The molecular basis of triazine-herbicide resistance in higher-plant chloroplasts

Joseph Hirschber; Anthony Bleecker; David J. Kyle; Lee McIntosh; Charles J. Arntzen

doi:10.1515/znc-1984-0521

The molecular basis of triazine-herbicide resistance in higher-plant chloroplasts

Joseph Hirschber, Anthony Bleecker, David J. Kyle, Lee McIntosh, Charles J. Arntzen

Research output: Contribution to journal › Article › peer-review

117 Scopus citations

Abstract

Triazine herbicides inhibit photosynthesis by blocking electron transport in photosystem II. The target site ofthe herbicide was identified as a chloroplast thylakoid polypeptide (the Q_B protein) of 32,000 daltons. Studies of triazine-resistant weed biotypes suggested that a subtle change in the Q_B protein caused the resistance. We have cloned the chloroplast gene (psbA) that codes this protein from herbicide-resistant and herbicide-susceptible biotypes of Solanum nigrum. By DN A sequencing we detected a single base substitution in the psbA gene of the resistant plants, resulting in an amino acid change (serine to glycine for the susceptible to resistance conversion). This mutation is exactly the same one which we have described in a herbicide-resistant biotype of Amaranthus hybridus.

Original language	English (US)
Pages (from-to)	412-420
Number of pages	9
Journal	Zeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume	39
Issue number	5
DOIs	https://doi.org/10.1515/znc-1984-0521
State	Published - May 1 1984
Externally published	Yes

Keywords

Chloroplasts
Molecular Basis of Herbicide-Resistance
Photosynthesis
Triazines

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1515/znc-1984-0521

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title = "The molecular basis of triazine-herbicide resistance in higher-plant chloroplasts",

abstract = "Triazine herbicides inhibit photosynthesis by blocking electron transport in photosystem II. The target site ofthe herbicide was identified as a chloroplast thylakoid polypeptide (the QB protein) of 32,000 daltons. Studies of triazine-resistant weed biotypes suggested that a subtle change in the QB protein caused the resistance. We have cloned the chloroplast gene (psbA) that codes this protein from herbicide-resistant and herbicide-susceptible biotypes of Solanum nigrum. By DN A sequencing we detected a single base substitution in the psbA gene of the resistant plants, resulting in an amino acid change (serine to glycine for the susceptible to resistance conversion). This mutation is exactly the same one which we have described in a herbicide-resistant biotype of Amaranthus hybridus.",

keywords = "Chloroplasts, Molecular Basis of Herbicide-Resistance, Photosynthesis, Triazines",

author = "Joseph Hirschber and Anthony Bleecker and Kyle, {David J.} and Lee McIntosh and Arntzen, {Charles J.}",

note = "Funding Information: This research was supported, in part, by a grant from CIBA-GEIGY, and DOE contract No. DEAC02-76ER01338 to Michigan State University.",

year = "1984",

month = may,

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doi = "10.1515/znc-1984-0521",

language = "English (US)",

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AU - Hirschber, Joseph

AU - Bleecker, Anthony

AU - Kyle, David J.

AU - McIntosh, Lee

AU - Arntzen, Charles J.

N1 - Funding Information: This research was supported, in part, by a grant from CIBA-GEIGY, and DOE contract No. DEAC02-76ER01338 to Michigan State University.

PY - 1984/5/1

Y1 - 1984/5/1

N2 - Triazine herbicides inhibit photosynthesis by blocking electron transport in photosystem II. The target site ofthe herbicide was identified as a chloroplast thylakoid polypeptide (the QB protein) of 32,000 daltons. Studies of triazine-resistant weed biotypes suggested that a subtle change in the QB protein caused the resistance. We have cloned the chloroplast gene (psbA) that codes this protein from herbicide-resistant and herbicide-susceptible biotypes of Solanum nigrum. By DN A sequencing we detected a single base substitution in the psbA gene of the resistant plants, resulting in an amino acid change (serine to glycine for the susceptible to resistance conversion). This mutation is exactly the same one which we have described in a herbicide-resistant biotype of Amaranthus hybridus.

AB - Triazine herbicides inhibit photosynthesis by blocking electron transport in photosystem II. The target site ofthe herbicide was identified as a chloroplast thylakoid polypeptide (the QB protein) of 32,000 daltons. Studies of triazine-resistant weed biotypes suggested that a subtle change in the QB protein caused the resistance. We have cloned the chloroplast gene (psbA) that codes this protein from herbicide-resistant and herbicide-susceptible biotypes of Solanum nigrum. By DN A sequencing we detected a single base substitution in the psbA gene of the resistant plants, resulting in an amino acid change (serine to glycine for the susceptible to resistance conversion). This mutation is exactly the same one which we have described in a herbicide-resistant biotype of Amaranthus hybridus.

KW - Chloroplasts

KW - Molecular Basis of Herbicide-Resistance

KW - Photosynthesis

KW - Triazines

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The molecular basis of triazine-herbicide resistance in higher-plant chloroplasts

Abstract

Keywords

ASJC Scopus subject areas

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