Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation. Export

@article{citeulike:2201639, abstract = {Bacteria play host to a wide range of protein phosphorylation-dephosphorylation systems (Fig. 1). As little as five years ago the known systems were thought to be late-emerging and absolutely prokaryote specific. Today we know that most protein kinases and protein phosphatases are descended from a set of common, and possibly quite ancient, prototypes. Prokaryote- and eukaryote-specific protein kinases and protein phosphatases are rare and represent exceptions, not the rule as previously thought. Commonality suggests that a dynamic and versatile regulatory mechanism was first adapted to the modulation of protein function as early if not earlier than more "basic" mechanisms such as allosterism, etc. The existence of common molecular themes confirms that the microbial world offers a unique, largely untapped library and a powerful set of tools for the understanding of a regulatory mechanism which is crucial to all organisms, tools whose diversity and experimental malleability will provide new avenues for exploring and understanding key modes of cellular regulation.}, address = {Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA. pjkennel@vt.edu}, author = {Kennelly, P. J. and Potts, M.}, citeulike-article-id = {2201639}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8759835}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8759835}, issn = {0021-9193}, journal = {J Bacteriol}, keywords = {kinase, phosphorylation, prokaryotic}, month = {August}, number = {16}, pages = {4759--4764}, posted-at = {2008-01-07 03:39:16}, priority = {2}, title = {Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8759835}, volume = {178}, year = {1996} }

TY - JOUR ID - citeulike:2201639 L3 - citeulike-article-id:2201639 N2 - Bacteria play host to a wide range of protein phosphorylation-dephosphorylation systems (Fig. 1). As little as five years ago the known systems were thought to be late-emerging and absolutely prokaryote specific. Today we know that most protein kinases and protein phosphatases are descended from a set of common, and possibly quite ancient, prototypes. Prokaryote- and eukaryote-specific protein kinases and protein phosphatases are rare and represent exceptions, not the rule as previously thought. Commonality suggests that a dynamic and versatile regulatory mechanism was first adapted to the modulation of protein function as early if not earlier than more "basic" mechanisms such as allosterism, etc. The existence of common molecular themes confirms that the microbial world offers a unique, largely untapped library and a powerful set of tools for the understanding of a regulatory mechanism which is crucial to all organisms, tools whose diversity and experimental malleability will provide new avenues for exploring and understanding key modes of cellular regulation. IS - 16 JF - J Bacteriol SN - 0021-9193 AD - Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA. pjkennel@vt.edu EP - 4764 TI - Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation. VL - 178 SP - 4759 KW - kinase KW - phosphorylation KW - prokaryotic AU - Kennelly, PJ AU - Potts, M PY - 1996/08// UR - http://view.ncbi.nlm.nih.gov/pubmed/8759835 ER -