C-TERMINAL TRUNCATION OF YEAST SERRS IS TOXIC FOR SACCHAROMYCES-CEREVISIAE DUE TO ALTERED MECHANISM OF SUBSTRATE RECOGNITION

Citation
B. Lenhard et al., C-TERMINAL TRUNCATION OF YEAST SERRS IS TOXIC FOR SACCHAROMYCES-CEREVISIAE DUE TO ALTERED MECHANISM OF SUBSTRATE RECOGNITION, FEBS letters, 439(3), 1998, pp. 235-240
Citations number
39
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
0014-5793
Volume
439
Issue
3
Year of publication
1998
Pages
235 - 240
Database
ISI
SICI code
0014-5793(1998)439:3<235:CTOYSI>2.0.ZU;2-S
Abstract
Like all other eukaryal cytosolic seryl-tRNA synthetase (SerRS) enzyme s, Saccharomyces cerevisiae SerRS contains a C-terminal extension not found in the enzymes of eubacterial and archaeal origin. Overexpressio n of C-terminally truncated SerRS lacking the 20-amino acid appended d omain (SerRSC20) is toxic to S. cerevisiae possibly because of altered substrate recognition. Compared to wild-type SerRS the truncated enzy me displays impaired tRNA-dependent serine recognition and is less sta ble. This suggests that the C-terminal peptide is important for the fo rmation or maintenance of the enzyme structure optimal for substrate b inding and catalysis. (C) 1998 Federation of European Biochemical Soci eties.