Mutations responsible for high light sensitivity in an atrazine-resistant mutant of Synechocystis 6714

The primary target of photoinhibition is the photosystem II reaction center. The process involves a reversible damage, followed by an irreversible inhibition of photosystem II activity. During cell exposition to high light intensity, the D1 protein is specially degraded. An atrazine-resistant mutant...

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Bibliographic Details
Published in:Plant molecular biology 1989-10, Vol.13 (4), p.355-363
Main Authors: KIRILOVSKY, D. L, GHADA AJLANI, PICAUD, M, ETIENNE, A.-L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Atrazine - pharmacology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cloning, Molecular
Cyanobacteria - drug effects
Cyanobacteria - genetics
Cyanobacteria - radiation effects
Drug Resistance, Microbial - genetics
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Genetics
Light
Mission oriented research
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Mutagenesis. Repair
Mutation
Photosystem II Protein Complex
Restriction Mapping
Synechocystis
Transformation, Genetic
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Summary:The primary target of photoinhibition is the photosystem II reaction center. The process involves a reversible damage, followed by an irreversible inhibition of photosystem II activity. During cell exposition to high light intensity, the D1 protein is specially degraded. An atrazine-resistant mutant of Synechocystis 6714, AzV, reaches the irreversible step of photoinhibition faster than wild-type cells. Two point mutations present in the psbA gene of AzV (coding for D1) lead to the modification of Phe 211 to Ser and Ala 251 to Val in D1. Transformation of wild-type cells with the AzV psbA gene shows that these two mutations are sufficient to induce a faster photodamage of PSII. Other DCMU- and/or atrazine-resistant mutants do not differ from the wild type when photoinhibited. We conclude that the QB pocket is involved in PSII photodamage and we propose that the mutation of Ala 251 might be related to a lower rate of proteolysis of the D1 protein than in the wild type.
ISSN:0167-4412
1573-5028
DOI:10.1007/BF00015547