Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-7-8
|
| pubmed:abstractText |
Microorganisms have developed three different systems for catalyzing protein phosphorylation and using this reversible modificaiton to regulate their cellular activities. The first 'classical' system utilizes nucleoside-triphosphates as phosphoryl donors and leads to the modification of protein substrates at serine/threonine or tyrosine residues. The second system, called 'two-component system', requires first a sensor kinase which autophosphorylates at a histidine residue at the expense of adenosine-triphosphate, then a response regulator which is modified in turn at an aspartate residue and thereafter induces a metabolic change within the cell. The third system, called 'PTS system', makes use of phosphoenol pyruvate to generate a phosphoryl group which is passed down a chain of several proteins and finally transferred to a sugar. There is increasing evidence that, contrary to an early concept, these systems and the corresponding enzymes (protein kinases and phosphoprotein phosphatases) share a number of structural and functional similarities with the phosphorylation-dephosphorylation machineries found in eukaryotes. Therefore one can expect that microorganisms will serve, once again, as a basic model for exploring and understanding a key regulatory mechanism, reversible protein phosphorylation, which concerns all organisms.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
80
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
43-8
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1998
|
| pubmed:articleTitle |
Post-translational modification of proteins by reversible phosphorylation in prokaryotes.
|
| pubmed:affiliation |
Institut de Biologie et Chimie des Protéines, CNRS, Lyon, France.
|
| pubmed:publicationType |
Journal Article,
Review
|