Pregled bibliografske jedinice broj: 490268
Old concepts - new insights in bacterial phosphorylation
Old concepts - new insights in bacterial phosphorylation // Summer Schools in Applied Molecular Microbiology:"Microbial Metabolites: Signals to Drugs"
Dubrovnik, Hrvatska, 2010. (pozvano predavanje, međunarodna recenzija, neobjavljeni rad, znanstveni)
CROSBI ID: 490268 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Old concepts - new insights in bacterial phosphorylation
Autori
Vujaklija, Dušica
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, neobjavljeni rad, znanstveni
Skup
Summer Schools in Applied Molecular Microbiology:"Microbial Metabolites: Signals to Drugs"
Mjesto i datum
Dubrovnik, Hrvatska, 21.08.2010. - 29.08.2010
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
bacterial phosphorylation; serine- threonine- and tyrosine-phosphorylated proteins
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
098-0982913-2877 - Temeljna molekularno-biološka istraživanja streptomiceta (Vujaklija, Dušica, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Dušica Vujaklija
(autor)