Naslov
Occurrence of protein disulfide bonds in different domains of life : a comparison of proteins from the Protein Data Bank

Autori
Bošnjak, Ivana ; Bojović, Viktor ; Šegvić-Bubić, Tanja ; Bielen, Ana

Izvornik
Protein engineering, design & selection (1741-0126) 27 (2014), 3; 65-72

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

Ključne riječi
Archaea; Bacteria; Eukarya; PDB; SS bond

Sažetak
Disulfide bonds (SS-bonds) are important posttranslational modifications of proteins. They stabilize a three-dimensional (3D) structure (structural SS-bonds) and have also the catalytic or regulatory functions (redox-active SS-bonds). Although SS-bonds are present in all groups of organisms, no comparative analyses of their frequency in proteins from different domains of life have been made to date. Using the Protein Data Bank (PDB), the number and subcellular locations of SS-bonds in Archaea, Bacteria, and Eukarya have been compared. Approximately three times higher frequency of proteins with SS-bonds in eukaryotic secretory organelles (e.g. endoplasmic reticulum) than in bacterial periplasmic/secretory pathways was calculated. Protein length also affects the SS-bond frequency: the average number of SS-bonds is positively correlated with the length for longer proteins (> 200 amino acids) while for the shorter and less stable proteins (< 200 amino acids) this correlation is negative. Medium size proteins (250 - 350 amino acids) indicated a high number of SS-bonds only in Archaea that could be explained by the need for additional protein stabilization in hyperthermophiles. The results emphasize higher capacity for the SS-bond formation and isomerization in Eukarya when compared to Archaea and Bacteria.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA