Naslov
Tyrosine phosphorylation of the proteins essential for the bacterial growth: the case of SSB protein

Autori
Paradžik Tina ; Hlevnjak Ana ; Kazazić Saša ; Filić Želimira ; Zahradka Davor ; Vujaklija Dušica

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Skup
Power of microbes in industry and environment 2016

Mjesto i datum
Krk, Hrvatska, 28.09.2016. - 01.10.2016

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
SSB; E.coli; phosphorylation

Sažetak
Protein tyrosine phosphorylation is an important way in life cycle regulation in eukaryotic cells, but this process has also been discovered in prokaryotes. Tyrosine modification has been shown to be involved in the regulation of bacterial exopolysaccharide biosynthesis and transport, but it has also some other important roles. Recently, MS analyses of the different bacterial phosphoproteomes revealed presence of proteins phosphorylated on tyrosine in all aspects of the cell metabolism. Single stranded DNA binding protein, which is essential for DNA metabolism, was found to be tyrosine phosphorylated. SSB needs to be removed and reattached to ssDNA during bacterial growth. This modification changes its affinity for DNA, and, therefore SSB phosphorylation could be involved in regulation of this process. This is general process in both Gram-positive and Gram- negative bacteria. Tyrosine phosphorylation of bacterial SSBs has been previously identified in Streptomyces sp, Bacillus subtilis and Escherichia coli. However, determination of the phosphorylation site and the extent of phosphorylation throughout the bacterial growth were analysed only for the SSB from B. subtilis. In this study we examined the extent of SSB phosphorylation in distantly related bacteria E. coli and S.coelicolor. In addition, we present the result of the MS analysis and discuss possible phosphorylation sites. The predicted phosphorylation sites were experimentally examined by the introduction of the point mutation on place of Tyr98 in E.coli SSB and on the place of Tyr 88 in S. coelicolor SSB using PCR-overlap mutagenesis.

Izvorni jezik
Engleski

Znanstvena područja
Biotehnologija

POVEZANOST RADA