Pulvomycin-resistant mutants of E.coli elongation factor Tu.
نویسندگان
چکیده
منابع مشابه
Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA.
Pulvomycin and the synonymous antibiotics labilomycin and 1063-Z are shown to inhibit prokaryotic protein synthesis by acting on elongation factor Tu (EF-Tu): in the presence of the antibiotic, the affinity of EF-Tu for guanine nucleotides is altered, the EF-Tu.GDP/GTP exchange is catalyzed, and the formation of the EF-Tu.GTP complex is stimulated. Hydrolysis of GTP by EF-Tu, induced by aminoac...
متن کاملInteraction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts.
Elongation factor (EF) Tu promotes the binding of aminoacyl-tRNA (aa-tRNA) to the acceptor site of the ribosome. This process requires the formation of a ternary complex (EF-Tu.GTP.aa-tRNA). EF-Tu is released from the ribosome as an EF-Tu.GDP complex. Exchange of GDP for GTP is carried out through the formation of a complex with EF-Ts (EF-Tu.Ts). Mammalian mitochondrial EF-Tu (EF-Tu(mt)) differ...
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The elongation factor EF-Tu is essential in bacterial translation and has sequences which are highly conserved even in phylogenetically distant bacteria. This allowed us to show that Gram negative bacteria had two copies of the tuf gene whereas most Gram positive bacteria including Mycobacteria had one copy of this gene (1). The agent of leprosy, Mycobacterium leprae, has been isolated from nat...
متن کاملPrimary 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 کاملDoc toxin is a kinase that inactivates elongation factor Tu.
The Doc toxin from bacteriophage P1 (of the phd-doc toxin-antitoxin system) has served as a model for the family of Doc toxins, many of which are harbored in the genomes of pathogens. We have shown previously that the mode of action of this toxin is distinct from the majority derived from toxin-antitoxin systems: it does not cleave RNA; in fact P1 Doc expression leads to mRNA stabilization. How...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1994
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1994.tb06840.x