Naslov
The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity

Autori
Weygand-Durasević, Ivana ; Lenhard, Boris ; Filipić, Sanda ; Söll, Dieter

Izvornik
Journal of biological chemistry (0021-9258) 271 (1996), 5; 2455-2461

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

Ključne riječi
Saccharomyces cerevisiae ; seryl-tRNA synthetase ; C-terminal extension

Sažetak
Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) contains a 20-amino acid C-terminal extension, which is not found in prokaryotic SerRS enzymes. A truncated yeast SES1 gene, lacking the 60 base pairs that encode this C-terminal domain, is able to complement a yeast SES1 null allele strain ; thus, the C-terminal extension in SerRS is dispensable for the viability of the cell. However, the removal of the C-terminal peptide affects both stability of the enzyme and its affinity for the substrates. The truncation mutant binds tRNA with 3.6-fold higher affinity, while the Km for serine is 4-fold increased relative to the wild-type SerRS. This indicates the importance of the C-terminal extension in maintaining the overall structure of SerRS.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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