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Amino acid sequence of elongation factor Tu. Characterization and alignment of the cyanogen bromide fragments and location of the cysteine residues
Author(s) -
Laursen Richard A.,
Nagarkatti Surekha,
Miller David L.
Publication year - 1977
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(77)80416-x
Subject(s) - cyanogen bromide , miller , cysteine , chemistry , sequence (biology) , library science , stereochemistry , computer science , peptide sequence , biochemistry , biology , ecology , gene , enzyme
Elongation factor Tu (EF-Tu) of E. coli possesses a remarkable variety of functions and properties. In addition to having a role in protein biosynthesis [l] , EF-Tu is a component of Q/3 RNA replicase [2] and a regulator of RNA polymerase activity [3] , and is coded for by two genes [4] . EF-Tu is also reported to be associated with membranes [5] and to have actin-like properties [6] . In conjunction with X-ray crystallographic studies currently in progress [7,8], we have undertaken the amino acid sequence analysis of EF-Tu. In this report we describe the sequence of nearly half the molecule, and discuss some tentative conclusions that can be made about its structure.