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Functional groups of elongation factor 2 involved in interactions with guanosine nucleotides and ribosomes
Author(s) -
Nurten Rüstem,
Aktar Neş'e Bilgin,
Bermek Engin
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80189-6
Subject(s) - ribosome , ternary complex , guanosine , nucleotide , guanine , chemistry , elongation factor , biochemistry , binding site , stereochemistry , rna , enzyme , gene
Treatment of rat liver EF‐2 with N ‐ethylmaleimide (MalNEt) did not affect the direct interactions of the factor with guanine nulceotides or with ribosomes, but inhibited the binding of guanosine 5′‐(β,γ‐methylene)triphosphate (GuoPP(CH 2 )P) to the EF‐2‐ribosome complex. The amino group reactive reagent 2,4,6‐trinitrobenzenesulfonate (TNBS), however, inhibited specifically the direct interactions of EF‐2 with guanine nucleotides, but not the binding of GuoPP(CH 2 )P to the EF‐2‐ribosome complex. The different sensitivities of EF‐2 to MalNEt and to TNBS suggested that the binding sites involved in the binary vs . ternary complex might correspond to different conformational states or might even be distinct physical entities.