Precursor for elongation factor Tu from Escherichia coli
نویسندگان
چکیده
منابع مشابه
Primary structure of elongation factor Tu from Escherichia coli.
The amino acid sequence of elongation factor Tu (EF-Tu) from Escherichia coli has been determined. EF-Tu is a single-chain polypeptide composed of 393 amino acids (Mr 43,225 for the species bearing COOH-terminal serine). The NH2-terminal serine is acetylated, and lysine-56 is partially methylated. The sites of facile tryptic cleavage are at arginines 44 and 58 and at lysine-263. The cysteinyl r...
متن کاملLack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli.
The GTP-bound form of elongation factor Tu (EF-Tu) brings aminoacylated tRNAs (aa-tRNA) to the A-site of the ribosome. EF-Tu binds all cognate elongator aa-tRNAs with highly similar affinities, and its weaker or tighter binding of misacylated tRNAs may discourage their participation in translation. Norvaline (Nva) is a non-proteinogenic amino acid that is activated and transferred to tRNALeu by...
متن کاملAminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu.
Eubacterial tmRNAs (10Sa RNAs) are unique because they function, at least in Escherichia coli, both as tRNA and mRNA (for a review, see Muto et al+, 1998)+ These ;360 6 40-nt-long RNAs are charged with alanine at their 39 ends by alanyl-tRNA synthetases or AlaRS (Komine et al+, 1994; Ushida et al+, 1994)+ Alanylation occurs thanks to the presence of the equivalent of the G3-U70 pair, the major ...
متن کاملRole of domains in Escherichia coli and mammalian mitochondrial elongation factor Ts in the interaction with elongation factor Tu.
Bovine mitochondrial elongation factor Ts (EF-Tsmt) stimulates the activity of Escherichia coli elongation factor Tu (EF-Tu). In contrast, E. coli EF-Ts is unable to stimulate mitochondrial EF-Tu. EF-Tsmt forms a tight complex with E. coli EF-Tu governed by an association constant of 8.6 x 10(10). This value is 100-fold stronger than the binding constant for the formation of the E. coli EF-Tu.T...
متن کاملThe identification of a domain in Escherichia coli elongation factor Tu that interacts with elongation factor Ts.
A method has been developed to search for the elongation factor Tu (EF-Tu) domain(s) that interact with elongation factor Ts (EF-Ts). This method is based on the suppression of Escherichia coli EF-Tu-dominant negative mutation K136E, a mutation that exerts its effect by sequestering EF-Ts. We have identified nine single-amino acid- substituted suppression mutations in the region 146-199 of EF-T...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1986
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.165.2.474-482.1986