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

Abstract:

: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-Tsmt were 5-10-fold less active in stimulating the activity of EF-Tumt. The double mutation completely abolished the activity of EF-Tsmt.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zhang Y,Li X,Spremulli LL

doi

10.1016/0014-5793(96)00789-2

subject

Has Abstract

pub_date

1996-08-12 00:00:00

pages

330-2

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00789-2

journal_volume

391

pub_type

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