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C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition (CROSBI ID 81220)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Lenhard, Boris ; Praetoruis-Ibba, Mette ; Filipić, Sanda ; Soll, Dieter ; Weygand-Đurašević, Ivana C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition // FEBS letters, 439 (1998), 3; 235-240. doi: 10.1016/S0014-5793(98)01376-3

Podaci o odgovornosti

Lenhard, Boris ; Praetoruis-Ibba, Mette ; Filipić, Sanda ; Soll, Dieter ; Weygand-Đurašević, Ivana

engleski

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.

aminoacyl-tRNA synthetases ; tRNA recognition ; toxicity ; tRNA-dependent amino acid recognition ; protein degradation

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Podaci o izdanju

439 (3)

1998.

235-240

objavljeno

0014-5793

1873-3468

10.1016/S0014-5793(98)01376-3

Povezanost rada

Biologija

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