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Tyrosine phosphorylation and bacterial virulence 被引量:2
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作者 Sarah E Whitmore Richard J Lamont 《International Journal of Oral Science》 SCIE CAS CSCD 2012年第1期1-6,共6页
Protein phosphorylation on tyrosine has emerged as a key device in the control of numerous cellular functions in bacteria.In this article,we review the structure and function of bacterial tyrosine kinases and phosphat... Protein phosphorylation on tyrosine has emerged as a key device in the control of numerous cellular functions in bacteria.In this article,we review the structure and function of bacterial tyrosine kinases and phosphatases.Phosphorylation is catalyzed by autophosphorylating adenosine triphosphate-dependent enzymes(bacterial tyrosine(BY) kinases) that are characterized by the presence of Walker motifs.The reverse reaction is catalyzed by three classes of enzymes:the eukaryotic-like phosphatases(PTPs) and dual-specific phosphatases;the low molecular weight protein-tyrosine phosphatases(LMW-PTPs);and the polymerase-histidinol phosphatases(PHP).Many BY kinases and tyrosine phosphatases can utilize host cell proteins as substrates,thereby contributing to bacterial pathogenicity.Bacterial tyrosine phosphorylation/dephosphorylation is also involved in biofilm formation and community development.The Porphyromonas gingivalis tyrosine phosphatase Ltp1 is involved in a restraint pathway that regulates heterotypic community development with Streptococcus gordonii.Ltp1 is upregulated by contact with S.gordonii and Ltp1 activity controls adhesin expression and levels of the interspecies signal AI-2. 展开更多
关键词 oral biofilm porphyromonas gingivalis streptococcus tyrosine phosphorylation virulence
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