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Pregled bibliografske jedinice broj: 610570

Substrate recognition and fidelity of maize seryl- tRNA synthetases


Rokov-Plavec, Jasmina; Lesjak, Sonja; Gruić- Sovulj, Ita; Močibob, Marko; Dulić, Morana; Weygand-Đurašević, Ivana
Substrate recognition and fidelity of maize seryl- tRNA synthetases // Archives of biochemistry and biophysics, 529 (2013), 2; 122-130 doi:10.1016/j.abb.2012.11.014 (međunarodna recenzija, članak, znanstveni)


Naslov
Substrate recognition and fidelity of maize seryl- tRNA synthetases

Autori
Rokov-Plavec, Jasmina ; Lesjak, Sonja ; Gruić- Sovulj, Ita ; Močibob, Marko ; Dulić, Morana ; Weygand-Đurašević, Ivana

Izvornik
Archives of biochemistry and biophysics (0003-9861) 529 (2013), 2; 122-130

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

Ključne riječi
Aminoacyl-tRNA synthetase; tRNA; editing; plant; mitochondria; chloroplast

Sažetak
Aminoacyl-tRNA synthetases (aaRSs) catalyze the attachment of amino acids to their cognate tRNAs to establish the genetic code. To obtain the high degree of accuracy that is observed in translation, these enzymes must exhibit strict substrate specificity for their cognate amino acids and tRNAs. We studied the requirements for tRNASer recognition by maize cytosolic seryl-tRNA synthetase (SerRS). The enzyme efficiently recognized bacterial and eukaryotic tRNAsSer indicating that it can accommodate various types of tRNASer structures. Discriminator base G73 is crucial for recognition by cytosolic SerRS. Although cytosolic SerRS efficiently recognized bacterial tRNAsSer, it is localized exclusively in the cytosol. The fidelity of maize cytosolic and dually targeted organellar SerRS with respect to amino acid recognition was compared. Organellar SerRS exhibited higher discrimination against tested non-cognate substrates as compared with cytosolic counterpart. Both enzymes showed pre- transfer editing activity implying their high overall accuracy. The contribution of various reaction pathways in the pre-transfer editing reactions by maize enzymes were different and dependent on the non-cognate substrate. The fidelity mechanisms of maize organellar SerRS, high discriminatory power and proofreading, indicate that aaRSs in general may play an important role in translational quality control in plant mitochondria and chloroplasts.

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


Uključenost u ostale bibliografske baze podataka:


  • BIOSIS Previews (Biological Abstracts)
  • CA Search (Chemical Abstracts)
  • EMBASE (Excerpta Medica)
  • MEDLINE
  • EMBiology
  • Research Alert
  • SCISEARCH


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