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Pregled bibliografske jedinice broj: 173005

Differential modes of transfer RNASer recognition in Methanosarcina barkeri


Korenčić, Dragana; Polycarpo, Carla; Weygand-Đurašević, Ivana; Söll, Dieter
Differential modes of transfer RNASer recognition in Methanosarcina barkeri // Journal of Biological Chemistry, 279 (2004), 48780-48786 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 173005 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Differential modes of transfer RNASer recognition in Methanosarcina barkeri

Autori
Korenčić, Dragana ; Polycarpo, Carla ; Weygand-Đurašević, Ivana ; Söll, Dieter

Izvornik
Journal of Biological Chemistry (0021-9258) 279 (2004); 48780-48786

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

Ključne riječi
tRNASer; seryl-tRNA synthetase; methanogenic archaea; identity elements

Sažetak
Two dissimilar seryl-tRNA synthetases (SerRSs) exist in Methanosarcina barkeri, one of bacterial type, and another resembling SerRSs present only in some methanogenic archaea. In order to investigate the requirements of these enzymes for tRNASer recognition, serylation of variant transcripts of M. barkeri tRNASer was kinetically analyzed in vitro with pure enzyme preparations. Characteristically for the serine system, the length of the variable arm was shown to be crucial for both enzymes, as was the identity of the discriminator base (G73). Moreover, a novel determinant for the specific tRNASer recognition was identified as the anticodon stem base pair G30:C40 ; its contribution to the efficiency of serylation was remarkable for both SerRSs. However, despite these similarities, the two SerRSs do not possess a uniform mode of tRNASer recognition, and additional determinants are necessary for serylation specificity by the methanogenic enzyme. In particular, the methanogenic SerRS relies on G1:C72 identity, and on the number of unpaired nucleotides at the base of the variable stem for tRNASer recognition, unlike its bacterial type counterpart. We propose that such a distinction between the two enzymes in tRNASer identity determinants reflects their evolutionary pathways, hence attesting to their diversity.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



POVEZANOST RADA


Projekti:
0119650

Ustanove:
Prirodoslovno-matematički fakultet, Zagreb

Profili:

Avatar Url Ivana Weygand Đurašević (autor)


Citiraj ovu publikaciju:

Korenčić, Dragana; Polycarpo, Carla; Weygand-Đurašević, Ivana; Söll, Dieter
Differential modes of transfer RNASer recognition in Methanosarcina barkeri // Journal of Biological Chemistry, 279 (2004), 48780-48786 (međunarodna recenzija, članak, znanstveni)
Korenčić, D., Polycarpo, C., Weygand-Đurašević, I. & Söll, D. (2004) Differential modes of transfer RNASer recognition in Methanosarcina barkeri. Journal of Biological Chemistry, 279, 48780-48786.
@article{article, author = {Koren\v{c}i\'{c}, Dragana and Polycarpo, Carla and Weygand-\DJura\v{s}evi\'{c}, Ivana and S\"{o}ll, Dieter}, year = {2004}, pages = {48780-48786}, keywords = {tRNASer, seryl-tRNA synthetase, methanogenic archaea, identity elements}, journal = {Journal of Biological Chemistry}, volume = {279}, issn = {0021-9258}, title = {Differential modes of transfer RNASer recognition in Methanosarcina barkeri}, keyword = {tRNASer, seryl-tRNA synthetase, methanogenic archaea, identity elements} }
@article{article, author = {Koren\v{c}i\'{c}, Dragana and Polycarpo, Carla and Weygand-\DJura\v{s}evi\'{c}, Ivana and S\"{o}ll, Dieter}, year = {2004}, pages = {48780-48786}, keywords = {tRNASer, seryl-tRNA synthetase, methanogenic archaea, identity elements}, journal = {Journal of Biological Chemistry}, volume = {279}, issn = {0021-9258}, title = {Differential modes of transfer RNASer recognition in Methanosarcina barkeri}, keyword = {tRNASer, seryl-tRNA synthetase, methanogenic archaea, identity elements} }

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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