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. 1993 Nov 1;90(21):9973–9977. doi: 10.1073/pnas.90.21.9973

Rapid interchange between two distinct forms of cyanobacterial photosystem II reaction-center protein D1 in response to photoinhibition.

A K Clarke 1, A Soitamo 1, P Gustafsson 1, G Oquist 1
PMCID: PMC47695  PMID: 8234343

Abstract

We have studied photoinhibition of photosynthesis in the cyanobacterium Synechococcus sp. PCC 7942, which possesses two distinct forms of the photosystem II reaction-center protein D1 (D1:1 and D1:2). We report here that when cells adapted to a growth irradiance of 50 mumol.m-2.s-1 are exposed to an irradiance of 500 mumol.m-2.s-1, the normally predominant D1 form (D1:1) is rapidly replaced with the alternative D1:2. This interchange is not only complete within the first hour of photoinhibition but is also fully reversible once cells are returned to 50 mumol.m-2 x s-1. By using a mutant that synthesizes only D1:1, we show that the failure to replace D1:1 with D1:2 during photoinhibition results in severe loss of photosynthetic activity as well as a diminished capacity to recover after the stress period. We believe that this interchange between D1 forms may constitute an active component in a protection mechanism unique among photosynthetic organisms that enables cyanobacteria to effectively cope with and recover from photoinhibition.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barber J., Andersson B. Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci. 1992 Feb;17(2):61–66. doi: 10.1016/0968-0004(92)90503-2. [DOI] [PubMed] [Google Scholar]
  2. Bouyoub A., Vernotte C., Astier C. Functional analysis of the two homologous psbA gene copies in Synechocystis PCC 6714 and PCC 6803. Plant Mol Biol. 1993 Jan;21(2):249–258. doi: 10.1007/BF00019941. [DOI] [PubMed] [Google Scholar]
  3. Bustos S. A., Golden S. S. Light-regulated expression of the psbD gene family in Synechococcus sp. strain PCC 7942: evidence for the role of duplicated psbD genes in cyanobacteria. Mol Gen Genet. 1992 Mar;232(2):221–230. doi: 10.1007/BF00280000. [DOI] [PubMed] [Google Scholar]
  4. Bustos S. A., Schaefer M. R., Golden S. S. Different and rapid responses of four cyanobacterial psbA transcripts to changes in light intensity. J Bacteriol. 1990 Apr;172(4):1998–2004. doi: 10.1128/jb.172.4.1998-2004.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clarke A. K., Critchley C. Synthesis of early heat shock proteins in young leaves of barley and sorghum. Plant Physiol. 1990 Oct;94(2):567–576. doi: 10.1104/pp.94.2.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Clarke A. K., Critchley C. The identification of a heat-shock protein complex in chloroplasts of barley leaves. Plant Physiol. 1992 Dec;100(4):2081–2089. doi: 10.1104/pp.100.4.2081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Golden S. S., Brusslan J., Haselkorn R. Expression of a family of psbA genes encoding a photosystem II polypeptide in the cyanobacterium Anacystis nidulans R2. EMBO J. 1986 Nov;5(11):2789–2798. doi: 10.1002/j.1460-2075.1986.tb04569.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Golden S. S., Cho D. S., Nalty M. S. Two functional psbD genes in the cyanobacterium Synechococcus sp. strain PCC 7942. J Bacteriol. 1989 Sep;171(9):4707–4713. doi: 10.1128/jb.171.9.4707-4713.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jansson C., Debus R. J., Osiewacz H. D., Gurevitz M., McIntosh L. Construction of an Obligate Photoheterotrophic Mutant of the Cyanobacterium Synechocystis 6803 : Inactivation of the psbA Gene Family. Plant Physiol. 1987 Dec;85(4):1021–1025. doi: 10.1104/pp.85.4.1021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Krupa Z., Oquist G., Gustafsson P. Photoinhibition and Recovery of Photosynthesis in psbA Gene-Inactivated Strains of Cyanobacterium Anacystis nidulans. Plant Physiol. 1990 May;93(1):1–6. doi: 10.1104/pp.93.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kulkarni R. D., Schaefer M. R., Golden S. S. Transcriptional and posttranscriptional components of psbA response to high light intensity in Synechococcus sp. strain PCC 7942. J Bacteriol. 1992 Jun;174(11):3775–3781. doi: 10.1128/jb.174.11.3775-3781.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kyle D. J., Ohad I., Arntzen C. J. Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes. Proc Natl Acad Sci U S A. 1984 Jul;81(13):4070–4074. doi: 10.1073/pnas.81.13.4070. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mattoo A. K., Pick U., Hoffman-Falk H., Edelman M. The rapidly metabolized 32,000-dalton polypeptide of the chloroplast is the "proteinaceous shield" regulating photosystem II electron transport and mediating diuron herbicide sensitivity. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1572–1576. doi: 10.1073/pnas.78.3.1572. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mulligan B., Schultes N., Chen L., Bogorad L. Nucleotide sequence of a multiple-copy gene for the B protein of photosystem II of a cyanobacterium. Proc Natl Acad Sci U S A. 1984 May;81(9):2693–2697. doi: 10.1073/pnas.81.9.2693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Samuelsson G., Lönneborg A., Gustafsson P., Oquist G. The Susceptibility of Photosynthesis to Photoinhibition and the Capacity of Recovery in High and Low Light Grown Cyanobacteria, Anacystis nidulans. Plant Physiol. 1987 Feb;83(2):438–441. doi: 10.1104/pp.83.2.438. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schaefer M. R., Golden S. S. Differential expression of members of a cyanobacterial psbA gene family in response to light. J Bacteriol. 1989 Jul;171(7):3973–3981. doi: 10.1128/jb.171.7.3973-3981.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Schaefer M. R., Golden S. S. Light availability influences the ratio of two forms of D1 in cyanobacterial thylakoids. J Biol Chem. 1989 May 5;264(13):7412–7417. [PubMed] [Google Scholar]
  18. Shipton C. A., Barber J. Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6691–6695. doi: 10.1073/pnas.88.15.6691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Vass I., Styring S., Hundal T., Koivuniemi A., Aro E., Andersson B. Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1408–1412. doi: 10.1073/pnas.89.4.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]

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