Nucleotide sequence ofMycobacterium lepraeelongation factor (EF-Tu) gene
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چکیده
منابع مشابه
Nucleotide sequence of Mycobacterium leprae elongation factor (EF-Tu) gene.
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 کاملCloning and nucleotide sequence of a tobacco chloroplast translational elongation factor, EF-Tu.
Translational elongation factor is an essential component for protein synthesis that functions by binding aminoacylated tRNAs to the ribosome-mRNA complex. This function is performed by EF-Tu in prokaryotes and eukaryotic organelles, and by EF-la in eukaryotes (for review see Miller and Weissbach, 1977). In lower photosynthetic eukaryotes, including Chlamydomonas (Baldauf and Palmer, 1990) and ...
متن کاملMechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base.
Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Similarly to other GTP-binding proteins, the structural changes in the P loop and the Mg(2+) binding site are known to be important for nucleotide release from EF-Tu. In the present paper, we determine the contribution of the contacts between helix D of EF-Tu at the base side of the nucleotide and ...
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Bacterial type VI secretion is an offensive and defensive weapon that utilizes a molecular warhead to inject toxins into neighboring cells. In this issue of Cell, Whitney et al. report a new class of toxin that disrupts the core metabolism of recipient cells and uncover a surprising requirement for EF-Tu.
متن کاملInteraction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.
The middle and C-terminal domain (domain II/III) of elongation factor Tu from Thermus thermophilus lacking the GTP/GDP binding domain have been prepared by treating nucleotide-free protein with Staphylococcus aureus V8 protease. The isolated domain II/III of EF-Tu has a compact structure and high resistance against tryptic treatment and thermal denaturation. As demonstrated by circular dichrois...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1993
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/21.14.3327