Pregled bibliografske jedinice broj: 584848
Can bacterial Hanks-type kinases constitute signal transduction cascades?
Can bacterial Hanks-type kinases constitute signal transduction cascades? // From Molecules to Life and Back / Dumić, Jerka ; Kovarnik Zrinka ; Varljen Jadranka (ur.).
Opatija: Hrvatsko Društvo za Biotehnologiju, 2012. str. 202-202 (poster, međunarodna recenzija, sažetak, znanstveni)
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Naslov
Can bacterial Hanks-type kinases constitute signal transduction cascades?
Autori
Dobrinić Paula ; Kobir Ahasanul ; Mijaković Ivan ; Franjević Damjan
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
From Molecules to Life and Back
/ Dumić, Jerka ; Kovarnik Zrinka ; Varljen Jadranka - Opatija : Hrvatsko Društvo za Biotehnologiju, 2012, 202-202
ISBN
978-953-95551-4-4
Skup
FEBS 3+Meeting
Mjesto i datum
Opatija, Hrvatska, 13.06.2012. - 16.06.2012
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
Bacterial Hanks-type kinases; protein kinase cascade; protein phosphorylation; signal transduction
Sažetak
Signal transduction in bacteria most often includes phosphorylation of histidine and aspartate residues, within relatively simple two-component systems. Some bacteria also possess serine/threonine-specific protein kinases, which belong to a large superfamily of Hanks-type kinases, together with the homologous eukaryotic enzymes. Aim of this research was to find out whether bacterial Hanks-type kinases constitute a phosphorylation cascade. Signal transduction through protein kinase cascades enables amplification of the signal and integration of different signalling pathways. This type of signal transduction is well studied and an important phenomenon in eukaryotes, where it regulates various cellular processes, but it hasn’t been associated with bacteria. A model Gram-positive bacterium Bacillus subtilis possesses a few Hanks-type kinases, two of them being membrane proteins. To determine whether these kinases phosphorylate each other, it was necessary to abolish their autophosphorylation activity. This was accomplished by site-directed mutagenesis of the active site. After expression and purification of recombinant proteins, in vitro phosphorylation assays with 32P-γ-ATP were performed. Wild-type and mutant forms of different kinases were combined. It was determined that both membrane-linked kinases, PrkC and YabT, phosphorylate a citosolic kinase YbdM. Also, intermolecular kinase activity of PrkC was confirmed. Structural resemblance of PrkC to eukaryotic receptor kinases and its ability to transphosphorylate, make this membrane kinase a good candidate for the first step of the newly characterized signal transduction cascade in bacteria.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
119-1193080-1214 - Molekularna filogenija, evolucija i simbioza slatkovodnih beskralježnjaka (Kalafatić, Mirjana, MZOS ) ( CroRIS)
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb