Pregled bibliografske jedinice broj: 480424
Two types of seryl-tRNA synthetase in methanogenic archaea
Two types of seryl-tRNA synthetase in methanogenic archaea // Molecular biology of archaea II
Cambridge, Ujedinjeno Kraljevstvo, 2010. (poster, nije recenziran, pp prezentacija, znanstveni)
CROSBI ID: 480424 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Two types of seryl-tRNA synthetase in methanogenic archaea
Autori
Lesjak, Sonja ; Weygand-Đurašević, Ivana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, pp prezentacija, znanstveni
Skup
Molecular biology of archaea II
Mjesto i datum
Cambridge, Ujedinjeno Kraljevstvo, 16.09.2010. - 19.09.2010
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
seryl-tRNA synthetase; methanogenic archaea; evolution
Sažetak
Methanogenic archaea are a polyphyletic group of methanogen producing archaea that can be divided into two classes: class I and class II. Methanogens employ two types of seryl-tRNA synthetase (SerRS), an enzyme essential for protein synthesis. Canonical (bacterial-type) SerRS occurs in majority of organisms including methanogens, while a highly diverged, structurally atypical, methanogenic-type SerRS is confined only to methanogenic archaea. Interestingly, both types of SerRS are equally distributed in class I and class II. The phylogenetic distribution of methanogenic-type SerRS coincides with the phylogenetic distribution of core methanogenesis enzymes, implying that metSerRS is endogenous in methanogens. Bacterial-type SerRS seems to be horizontally transferred from bacteria, archaea or eukaryotes. Since archaeon Methanosarcina barkeri contains both types of SerRS, which were structurally and functionally well characterized in our laboratory, we set out to develop an in vivo system in E. coli for studying archaeal tRNA serylation by both enzymes. We show that co-expression of M. barkeri SerRS gene, encoding bacterial- or methanogenic-type SerRS (mMbSerRS), with the gene for archaeal suppressor tRNA(CGA) leads to suppression of bacterial amber mutations. The efficiency of suppression by mMbSerRS variants faithfully reflects enzymes' serylation propensity obtained by in vitro kinetic measurements, confirming the importance of idiosyncratic structural features.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
POVEZANOST RADA
Projekti:
119-0982913-1358 - Strukturna raznolikost seril-tRNA sintetaza i točnost biosinteze proteina (Rokov Plavec, Jasmina; Weygand Đurašević, Ivana, MZOS ) ( CroRIS)
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb