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