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ABSTRACT: Aims
Protein phosphorylation is a principal signaling mechanism that mediates regulation of enzymatic activities, modulation of gene expression, and adaptation to environmental changes. Recent studies have shown a ubiquitous distribution of eukaryotic-type Serine/Threonine protein kinases in prokaryotic genomes, though the functions, substrates, and possible regulation of these enzymes remain largely unknown. In this study, we investigated whether cyanobacterial protein phosphorylation may be subject to redox regulation through modulation of the cysteine redox state, as has previously been reported for animals and plants. We also explored the role of a cyanobacterial Serine/Threonine kinase in oxidative stress tolerance.Results
The Synechocystis sp. PCC 6803 Serine/Threonin
SUBMITTER: Mata-Cabana A
PROVIDER: S-EPMC3373224 | biostudies-literature | 2012 Aug
REPOSITORIES: biostudies-literature