C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition.
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.
Lenhard
B
B
Department of Chemistry, Faculty of Science, University of Zagreb, Croatia.
Praetorius-Ibba
M
M
Filipic
S
S
Söll
D
D
Weygand-Durasevic
I
I
D000595:Amino Acid Sequence; D004271:DNA, Fungal / Q000378:metabolism*; D004795:Enzyme Stability; D007700:Kinetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012362:RNA, Transfer, Ser / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D012714:Serine-tRNA Ligase / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D013379:Substrate Specificity
D004271:DNA, Fungal; D012362:RNA, Transfer, Ser; D012714:Serine-tRNA Ligase