Protein phosphorylation on Ser, Thr and Tyr residues in cyanobacteria.
Cyanobacteria belong to an extremely diverse group of gram-negative prokaryotes. They are all able to perform oxygen-evolving photosynthesis, but differ in morphology, ecological habitats, and physiology. This diversity is also reflected in the complexity of regulatory proteins involved in protein phosphorylation on Ser, Thr and Tyr residues. For those strains whose genomes are completely sequenced, for example, the number of genes identified so far that encode Ser/Thr and Tyr kinases range from none to 52. Genetic, molecular as well as functional genomic analyses demonstrate that Ser/Thr and Tyr kinases and phosphatases are involved in the regulation of a variety of activities according to changes in growth conditions or cell metabolism, such as cell motility, carbon and nitrogen metabolism, photosynthesis and stress response. The major challenge in the near future is to integrate these components into signaling pathways and identify their targets. Some of the Ser/Thr and Tyr kinases and phosphatases are expected to interact with classical two-component signaling pathways.
Zhang
Cheng-Cai
CC
National Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, Hubei, China. cczhang@ibsm.cnrs-mrs.fr
Jang
Jichan
J
Sakr
Samer
S
Wang
Li
L
D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000378:metabolism; D002465:Cell Movement; D000458:Cyanobacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D015398:Signal Transduction
D001426:Bacterial Proteins; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases