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Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes

by: Roman Sobotka, Ulf Dühring, Josef Komenda, Enrico Peter, Zdenko Gardian, Martin Tichy, Bernhard Grimm, and Annegret Wilde

In: The Journal of Biological Chemistry (July 2008) .

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URL:	http://www.ncbi.nlm.nih.gov/pubmed/18625715
DOI:

Gun4 is a porphyrin binding protein that activates magnesium chelatase, a multimeric enzyme catalyzing the first committed step in chlorophyll biosynthesis. In plants, GUN4 has been implicated in plastid-to-nucleus retrograde signalling processes that coordinate both photosystem II and photosystem I nuclear gene expression with chloroplast function. In this work we present the functional analysis of Gun4 from the cyanobacterium Synechocystis sp. PCC 6803. Affinity co-purification of the FLAG-tagged Gun4 with the ChlH subunit of the magnesium chelatase confirmed the association of Gun4 with the enzyme in cyanobacteria. Inactivation of the gun4 gene abolished photoautotrophic growth of the resulting gun4 mutant strain that exhibited a decreased activity of magnesium chelatase. Consequently, the cellular content of chlorophyll-binding proteins was highly inadequate, especially that of proteins of photosystem II. Immunoblot analyses, blue native polyacrylamide gel electrophoresis and radiolabeling of the membrane protein complexes suggested that the availability of the photosystem II antenna protein CP47 is a limiting factor for the photosystem II assembly in the gun4 mutant.

BibTeX record

@article{sobotka_importance_2008,
  abstract = {Gun4 is a porphyrin binding protein that activates magnesium chelatase, a multimeric enzyme catalyzing the first committed step in chlorophyll biosynthesis. In plants, GUN4 has been implicated in plastid-to-nucleus retrograde signalling processes that coordinate both photosystem II and photosystem I nuclear gene expression with chloroplast function. In this work we present the functional analysis of Gun4 from the cyanobacterium Synechocystis sp. PCC 6803. Affinity co-purification of the FLAG-tagged Gun4 with the ChlH subunit of the magnesium chelatase confirmed the association of Gun4 with the enzyme in cyanobacteria. Inactivation of the gun4 gene abolished photoautotrophic growth of the resulting gun4 mutant strain that exhibited a decreased activity of magnesium chelatase. Consequently, the cellular content of chlorophyll-binding proteins was highly inadequate, especially that of proteins of photosystem II. Immunoblot analyses, blue native polyacrylamide gel electrophoresis and radiolabeling of the membrane protein complexes suggested that the availability of the photosystem II antenna protein CP47 is a limiting factor for the photosystem II assembly in the gun4 mutant.},
  added-at = {2008-08-08T13:57:07.000+0200},
  author = {Sobotka, Roman and Dühring, Ulf and Komenda, Josef and Peter, Enrico and Gardian, Zdenko and Tichy, Martin and Grimm, Bernhard and Wilde, Annegret},
  biburl = {http://www.bibsonomy.org/bibtex/261fcd468696964b95bbfbe6ad871ebac/microbio},
  doi = {M803787200},
  interhash = {2c0eb39e61b3920664edb902977ee1b3},
  intrahash = {61fcd468696964b95bbfbe6ad871ebac},
  issn = {0021-9258},
  journal = {The Journal of Biological Chemistry},
  keywords = {imported},
  month = {July},
  note = {PMID: 18625715},
  timestamp = {2008-08-08T13:57:07.000+0200},
  title = {Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes},
  url = {http://www.ncbi.nlm.nih.gov/pubmed/18625715},
  year = 2008
}

Endnote record

%0 Journal Article
%1 sobotka_importance_2008
%A Sobotka, Roman
%A Dühring, Ulf
%A Komenda, Josef
%A Peter, Enrico
%A Gardian, Zdenko
%A Tichy, Martin
%A Grimm, Bernhard
%A Wilde, Annegret
%D 2008
%J The Journal of Biological Chemistry
%K 
%T Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes
%R M803787200
%U http://www.ncbi.nlm.nih.gov/pubmed/18625715
%X Gun4 is a porphyrin binding protein that activates magnesium chelatase, a multimeric enzyme catalyzing the first committed step in chlorophyll biosynthesis. In plants, GUN4 has been implicated in plastid-to-nucleus retrograde signalling processes that coordinate both photosystem II and photosystem I nuclear gene expression with chloroplast function. In this work we present the functional analysis of Gun4 from the cyanobacterium Synechocystis sp. PCC 6803. Affinity co-purification of the FLAG-tagged Gun4 with the ChlH subunit of the magnesium chelatase confirmed the association of Gun4 with the enzyme in cyanobacteria. Inactivation of the gun4 gene abolished photoautotrophic growth of the resulting gun4 mutant strain that exhibited a decreased activity of magnesium chelatase. Consequently, the cellular content of chlorophyll-binding proteins was highly inadequate, especially that of proteins of photosystem II. Immunoblot analyses, blue native polyacrylamide gel electrophoresis and radiolabeling of the membrane protein complexes suggested that the availability of the photosystem II antenna protein CP47 is a limiting factor for the photosystem II assembly in the gun4 mutant.

BibSonomy :: publication ::

Importance of the cyanobacterial Gun4 protein for chlorophyll metabolism and assembly of photosynthetic complexes

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