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Recognition between tRNASer and archaeal seryl-tRNA synthetases monitored by suppression of bacterial amber mutations


Lesjak, Sonja; Weygand-Đurašević, Ivana
Recognition between tRNASer and archaeal seryl-tRNA synthetases monitored by suppression of bacterial amber mutations // FEMS Microbiology Letters, 294 (2009), 1; 111-118 doi:10.1111/j.1574-6968.2009.01560.x (međunarodna recenzija, članak, znanstveni)


Naslov
Recognition between tRNASer and archaeal seryl-tRNA synthetases monitored by suppression of bacterial amber mutations

Autori
Lesjak, Sonja ; Weygand-Đurašević, Ivana

Izvornik
FEMS Microbiology Letters (0378-1097) 294 (2009), 1; 111-118

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

Ključne riječi
Seryl-tRNA synthetase; amber suppression; methanogenic archaea

Sažetak
Two dissimilar seryl-tRNA synthetases (SerRSs) exist in Methanosarcina barkeri: one of bacterial type (bMbSerRS) and the other resembling SerRSs present only in methanogenic archaea (mMbSerRS). While the expression of the archaeal bMbSerRS gene in Escherichia coli complements the function of thermolabile SerRS at a nonpermissive temperature, mMbSerRS does not. Our recent X-ray structural analysis of mMbSerRS revealed an idiosyncratic N-terminal domain and a catalytic zinc ion in the active site, identifying methanogenic-type SerRSs as atypical members of the SerRS family. To shed further light on substrate discrimination by methanogenic-type SerRS, we developed an in vivo system in E. coli to study tRNA serylation by mMbSerRS variants.We show that coexpression of the M. barkeri SerRS gene, encoding either bacterial- or methanogenic-type SerRS, with the gene for cognate archaeal suppressor tRNA leads to suppression of bacterial amber mutations, implying that the E. coli translation machinery can use serylated tRNA from methanogenic archaea as a substrate in protein synthesis. Furthermore, because serylation of M. barkeri serine-specific tRNA by endogenous E. coli SerRS is negligible, suppression is entirely dependent on recognition between archaeal partners (mMbSerRS/suppressor tRNASer). Thus, the efficiency of suppression by mMbSerRS variants quantified in the described b-galactosidasebased reporter system, accurately reflects enzymes’ serylation propensity obtained by in vitro kinetic measurements.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Projekt / tema
119-0982913-1358 - Strukturna raznolikost seril-tRNA sintetaza i točnost biosinteze proteina (Jasmina Rokov Plavec, )

Ustanove
Prirodoslovno-matematički fakultet, Zagreb

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


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