C‐terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition

FEBS Letters

Lenhard, Boris¹  Prætorius-Ibba, Mette²  Söll, Dieter²  Filipic, Sanda¹  Weygand-Durasevic, Ivana¹ 

[1] Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia;Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA

关键词: Aminoacyl-tRNA synthetase;    tRNA recognition;    Toxicity;    tRNA-dependent amino acid recognition;    Protein degradation;   

DOI  :  10.1016/S0014-5793(98)01376-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Like all other eukaryal cytosolic seryl-tRNA synthetase (SerRS) enzymes, Saccharomyces cerevisiae SerRS contains a C-terminal extension not found in the enzymes of eubacterial and archaeal origin. Overexpression of C-terminally truncated SerRS lacking the 20-amino acid appended domain (SerRSC20) is toxic to S. cerevisiae possibly because of altered substrate recognition. Compared to wild-type SerRS the truncated enzyme displays impaired tRNA-dependent serine recognition and is less stable. This suggests that the C-terminal peptide is important for the formation or maintenance of the enzyme structure optimal for substrate binding and catalysis.

【 授权许可】

Unknown