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

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

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

Izvornik
Book of abstracts of FEBS EMBO 2014 Conference / - , 2014

Skup
FEBS EMBO 2014 Conference

Mjesto i datum
Pariz, Francuska, 30.08.2014. - 04.09.2014

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Disulfide bonds; Domains of life; PDB

Sažetak
Disulfide bonds (SS bonds) are important post-translational modifications of proteins. They stabilize a three-dimensional structure (structural SS bonds) and also have 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, 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-sized proteins (250–350 amino acids) indicated a high number of SS bonds only in Archaea which 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 with Archaea and Bacteria.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija, Poljoprivreda (agronomija)

POVEZANOST RADA