Anacystis Mutants with Different Tolerances to DCMU-Type Herbicides Show Differences in Architecture and Dynamics of the Photosynthetic Apparatus, Depending on Site and Mode of the Amino Acid Exchanges in the D1 Protein

Mutants of Anacystis R2 with different amino acid exchanges in positions 255 and/or 264 in copy I of the psbA gene, leading to different tolerances to DCMU-type herbicides, are com- pared with the respective wild type concerning pigmentation and incorporation of 35S into the D1 protein upon growth in the presence of [35S]methionine. All mutants have shade-type appearance compared to the wild type, although to different extents depending on site and mode of the amino acid exchange in the D1 protein. Except for 3 mutants, there is no correlation between shade-type appearance on one hand and resistance towards a certain inhibitor on the other hand. Not only the molar ratio of phycocyanin (PC) to chlorophyll (Chi) is higher in all mutants compared to the respective wild type, but also the rate of synthesis of the D1 protein. On the background of different levels of total 35S incorporation within 18 min, D1 synthesis can be related to shade adaptation. Degradation of the D1 protein remains to be thoroughly studied in this context. No reproducible differences in whole chain electron transport were observed between mutants and wild type.

• Publication year

  1990

• Venue

  Zeitschrift für Naturforschung C - A Journal of Biosciences

• Publication date

  1990-05-01

• Fields of study

  Biology, Medicine, Environmental Science

• Identifiers
  DOI 10.1515/znc-1990-0523PMID 2116130
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Dynamics of the photosystem II reaction center.

  1989cited by this paper
• The QB site modulates the conformation of the photosystem II reaction center polypeptides

  1988cited by this paper
• Determination of the Rate Limiting Step for Photosynthesis in a Nearly Isonuclear Rapeseed (Brassica napus L.) Biotype Resistant to Atrazine.

  1988cited by this paper
• Characterization of the photosystem II 32 kDa protein in Synechococcus PCC7942

  1988cited by this paper
• Molecular genetics of herbicide resistance in cyanobacteria

  1988cited by this paper
• Genetic analysis of two new mutations resulting in herbicide resistance in the cyanobacterium Synechcoccus sp. PCC 7002

  1988cited by this paper
• Triazine Resistance without Reduced Vigor in Phalaris paradoxa.

  1987cited by this paper
• Characterization of Triazine-Resistant and -Susceptible Isolines of Canola (Brassica napus L.).

  1986cited by this paper
• Expression of a family of psbA genes encoding a photosystem II polypeptide in the cyanobacterium Anacystis nidulans R2.

  1986cited by this paper
• Mutation to herbicide resistance maps within the psbA gene of Anacystis nidulans R2.

  1985cited by this paper
• Herbicide Resistance and Cross-Resistance: Changes at Three Distinct Sites in the Herbicide-Binding Protein

  1985cited by this paper
• Molecular Basis of Herbicide Resistance in Amaranthus hybridus

  1983cited by this paper

• General effect of photosynthetic electron transport inhibitors on translation precludes their use for investigating regulation of D1 biosynthesis in Synechococcus sp. strain PCC 7942

  2004cites this paper
• Eukaryotic Algae, Cyanobacteria and Pesticides

  2001cites this paper
• D1 polypeptide degradation may regulate psbA gene expression at transcriptional and translational levels in Synechocystis sp. PCC 6803

  1996cites this paper
• Effect of Different Concentrations of Atrazine on RC II-D1 Protein Synthesis and Cell Division in Anacystis in Strong White Light

  1995cites this paper
• Light-Responsive Gene Expression and the Biochemistry of the Photosystem II Reaction Center

  1994cites this paper
• Development of Shade-Type Appearance — Light Intensity Adaptation — and Regulation of the D1 Protein in Synechococcus

  1992cites this paper
• Amino Acid Substitutions in the D1 Protein of Photosystem II Affect QB-Stabilization and Accelerate Turnover of D1

  1990cites this paper