Pregled bibliografske jedinice broj: 327287
Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family
Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family // Journal of Biological Chemistry, 282 (2007), 3; 1882-1890 doi:10.1074/jbc.M609598200 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 327287 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family
Autori
Bredemeier, Rolf ; Schlegel, Thomas ; Ertel, Franziska ; Vojta, Aleksandar ; Borissenko, Ljudmila ; Bohnsack, Markus T. ; Groll, Michael ; von Haeseler, Arndt ; Schleiff, Enrico
Izvornik
Journal of Biological Chemistry (0021-9258) 282
(2007), 3;
1882-1890
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
beta-barrel; Omp85
Sažetak
Beta-Barrel-shaped channels of the Omp85 family are involved in the translocation or assembly of proteins of bacterial, mitochondrial, and plastidic outer membranes. We have compared these proteins to understand the evolutionary development of the translocators. We have demonstrated that the proteins from proteobacteria and mitochondria have a pore diameter that is at least five times smaller than found for the Omp85 in cyanobacteria and plastids. This finding can explain why Omp85 from cyanobacteria (but not the homologous protein from proteobacteria) was remodeled to become the protein translocation pore after endosymbiosis. Further, the pore-forming region of the Omp85 proteins is restricted to the C terminus. Based on a phylogenetic analysis we have shown that the pore-forming domain displays a different evolutionary relationship than the N-terminal domain. In line with this, the affinity of the N-terminal domain to the C-terminal region of the Omp85 from plastids and cyanobacteria differs, even though the N-terminal domain is involved in gating of the pore in both groups. We have further shown that the N-terminal domain of nOmp85 takes part in homo-oligomerization. Thereby, the differences in the phylogeny of the two domains are explained by different functional constraints acting on the regions. The pore-forming domain, however, is further divided into two functional regions, where the distal C terminus itself forms a dimeric pore. Based on functional and phylogenetic analysis, we suggest an evolutionary scenario that explains the origin of the contemporary translocon.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
053-1780469-2110 - Normizacija nekih pokazatelja zdravlja hrvatskih izvornih pasmina ovaca (Šimpraga, Miljenko, MZOS ) ( CroRIS)
Ustanove:
Veterinarski fakultet, Zagreb
Profili:
Aleksandar Vojta
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE