Similarities and Singularities of Three DnaK Proteins from the Cyanobacterium Synechocystis sp PCC 6803

被引:23
作者
Rupprecht, Eva [1 ]
Dueppre, Eva [1 ,2 ]
Schneider, Dirk [1 ,2 ]
机构
[1] Univ Freiburg, ZBMZ, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Johannes Gutenberg Univ Mainz, Inst Pharm & Biochem, D-55128 Mainz, Germany
关键词
DnaK; GrpE; Heat stress; Stress response; Synechocystis; MOLECULAR CHAPERONE SYSTEM; HEAT-SHOCK RESPONSE; SP STRAIN PCC-6803; ESCHERICHIA-COLI; NUCLEOTIDE EXCHANGE; PROTEOME ANALYSIS; HSP70; CHAPERONES; MECHANISM; SEQUENCE; LIGHT;
D O I
10.1093/pcp/pcq074
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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.
引用
收藏
页码:1210 / 1218
页数:9
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