Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange

FEBS Letters

Spremulli, Linda L.¹  Zhang, Yuelin¹  Li, Xin¹ 

[1] Department of Chemistry, Campus Box No. 3290, University of North Carolina, Chapel Hill, NC 27599-3290, USA

关键词: Protein synthesis;    Elongation factor;    Mitochondria;    Elongation factor Tu;    Elongation factor Ts;   

DOI  :  10.1016/0014-5793(96)00789-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg²⁺ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2–3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Ts_mt were 5–10-fold less active in stimulating the activity of EF-Tu_mt. The double mutation completely abolished the activity of EF-Ts_mt.

【 授权许可】

Unknown