Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome - PubMed (original) (raw)
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Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome
C C Zhang et al. Nucleic Acids Res. 1998.
Abstract
Bacteria usually use two-component systems for signal transduction, while eukaryotic organisms employ Ser/Thr and Tyr kinases and phosphatases for the same purpose. Many prokaryotes turn out to harbor Ser/Thr and Tyr kinases, Ser/Thr and Tyr phosphatases, and their accessory components as well. The sequence determination of the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 offers the possibility to survey the extent of such molecules in a prokaryotic organism. This cyanobacterium possesses seven Ser/Thr kinases, seven Ser/Thr and Tyr phosphatases, one protein kinase interacting protein, one protein kinase regulatory subunit and several WD40-repeat-containing proteins. The majority of the protein phosphatases presented in this study were previously reported as hypothetical proteins. We analyze here the structure and genetic organization of these ORFs in the hope of providing a guidance for their functional analysis. Unlike their eukaryotic counterparts, many of these genes are clustered on the chromosome, and this genetic organization offers the opportunity to study their possible interaction. In several cases, genes of two-component transducers are found within the same cluster as those encoding a Ser/Thr kinase or a Ser/Thr phosphatase; the implication for signal transduction mechanism will be discussed.
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References
- Nature. 1983 Feb 17-23;301(5901):623-6 - PubMed
- Mol Gen Genet. 1998 Apr;258(1-2):26-33 - PubMed
- Science. 1988 Jul 1;241(4861):42-52 - PubMed
- EMBO J. 1988 Jun;7(6):1853-62 - PubMed
- J Bacteriol. 1990 Apr;172(4):1998-2004 - PubMed
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