Naslov
Variations in amino acid composition in bacterial single stranded DNA–binding proteins correlate with GC content

Autori
Paradžik, Tina ; Filić, Želimira ; Vujaklija, Dušica

Izvornik
Periodicum biologorum (0031-5362) 118 (2016), 4; 385-397

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
SSB proteins, amino acid composition, GC content

Sažetak
Background and purpose SSB proteins are essential for the maintenance of the genome in all domains of life. Most bacterial SSBs are active as homotetramers. Each monomer consists of a highly conserved N-terminal domain (OB-fold) which is responsible for ssDNA binding and a disordered C-terminal (Ct) domain with a conserved acidic tail responsible for protein interactions and cooperative binding to ssDNA. The variations in these essential proteins prompted us to conduct an in silico analyses of the aa composition and properties of two distinct SSB domains in relation to bacterial GC content. Materials and methods SSB sequences were collected from genomes covering a wide range of GC content from 14 bacterial phyla. The ML trees were constructed for SSB sequences and corresponding 16S rRNA genes. The aa content of OB folds and Ct regions were subsequently analysed. Results SSB protein sequence analysis suggested a correlation between aa composition and GC content. We show how two distinct domains of SSB exhibit significant difference to the expected aa composition for a range of GC contents. In this respect we demonstrated that OB fold are less effected than Ct domain in a lane with its core function. Conclusions The aa composition of the OB fold and Ct domains in bacterial SSBs’ correlates with different GC ratios of bacteria. These changes are more pronounced in the SSB Ct domain. Consequently, this influences to a greater extent the biochemical properties of the Ct domains.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Računarstvo

POVEZANOST RADA