Journal Article

Similarities and Singularities of Three DnaK Proteins from the Cyanobacterium <i>Synechocystis</i> sp. PCC 6803

Eva Rupprecht, Eva Düppre and Dirk Schneider

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 51, issue 7, pages 1210-1218
Published in print July 2010 | ISSN: 0032-0781
Published online May 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq074
Similarities and Singularities of Three DnaK Proteins from the Cyanobacterium Synechocystis sp. PCC 6803

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  • Molecular and Cell Biology
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In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exchange factor. A comparative analysis indicates that DnaK2 is the most abundant DnaK protein in Synechocystis cells and only the expression of dnaK2 is highly up-regulated under various stress conditions. Finally, we show that a small amino acid motif, which is typically conserved at the very C-terminus of cyanobacterial DnaK3 proteins, is essential for the DnaK3 in vivo function.

Keywords: DnaK; GrpE; Heat stress; Stress response; Synechocystis

Journal Article.  5293 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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