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

Publisher Website
Google Scholar
Abstract
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.