Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria
Author:
Affiliation:
1. Department of Microbiology and Immunology, College of Physicians and Surgeons, Columbia University, New York, New York 10032
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology,Infectious Diseases
Link
https://journals.asm.org/doi/pdf/10.1128/MMBR.00042-10
Reference203 articles.
1. Absalon, C., et al. 2009. CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155:932-943.
2. The GTPase CpgA Is Implicated in the Deposition of the Peptidoglycan Sacculus in Bacillus subtilis
3. Adler, E., A. Donella-Deana, F. Arigoni, L. A. Pinna, and P. Stragler. 1997. Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases. Mol. Microbiol. 23:57-62.
4. Alber, T. 2009. Signaling mechanisms of the Mycobacterium tuberculosis receptor Ser/Thr protein kinases. Curr. Opin. Struct. Biol. 19:650-657.
5. Alexander, C., et al. 1995. Phosphorylation of elongation factor Tu prevents ternary complex formation. J. Biol. Chem. 270:14541-14547.
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