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Old concepts - new insights in bacterial phosphorylation (CROSBI ID 568322)

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Vujaklija, Dušica Old concepts - new insights in bacterial phosphorylation // Summer Schools in Applied Molecular Microbiology:"Microbial Metabolites: Signals to Drugs" Dubrovnik, Hrvatska, 21.08.2010-29.08.2010

Podaci o odgovornosti

Vujaklija, Dušica

engleski

Old concepts - new insights in bacterial phosphorylation

Introduction to phosphorylation: Reversible phosphorylation of proteins occurs in all organisms and possesses crucial regulatory roles in a broad spectrum of biological processes. Retrospective: It was discovered in the mid 1950s and for many years it was tought to exist only in eukaryotes. Period of controversy: Serine, threonine and tyrosine phosphorylation is the most common type of phosphorylation in eukaryotes, on contrary, in bacteria phosphorylation occurs predominantly on histidine and aspartate (two-component system). Until the early 1990s it was largely considered that these two phosphorylation systems are mutually exclusive. Two-component systems: Crucial bacterial regulatory mechanism for sensing and responding to internal and external signals. It also regulates different functions related to bacterial pathogenicity: including toxin production, cell adhesion, quorum sensing, capsule synthesis, motility, and drug resistance. More recent data: Genome sequencing confirmed the widespread presence of genes encoding eukaryotic like Ser/Thr kinases and phosphatases. Tyrosine phosphorylation in bacteria: The first studies only suggested tyrosine kinase activities in bacteria, but the first conclusive evidence of bacterial tyrosine phosphorylation came only a decade ago. Bacterial tyrosine kinases exibit unexpected features and have been identified in a variety of bacteria. The list of substrates of BY-kinases is increasing and will be discussed with emphasis on tyrosine phosphorylation of bacterial single stranded DNA binding proteins, particularly SSB proteins from Streptomyces sp. Powerful new methods: the number of serine-threonine- and tyrosine-phosphorylated proteins have been discovered recently by mass spectrometry-based gel-free phosphoproteomics.

bacterial phosphorylation; serine- threonine- and tyrosine-phosphorylated proteins

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Podaci o prilogu

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Podaci o skupu

Summer Schools in Applied Molecular Microbiology:"Microbial Metabolites: Signals to Drugs"

pozvano predavanje

21.08.2010-29.08.2010

Dubrovnik, Hrvatska

Povezanost rada

Biologija