Functional Interaction of Mammalian Valyl-tRNA Synthetase with Elongation Factor EF-1α in the Complex with EF-1H
                    
                        
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                    چکیده
منابع مشابه
Interaction of eukaryote elongation factor EF 1 with guanosine nucleotides and aminoacyl-tRNA.
Evidence for two species of elongation factor 1 (EF 1(A) and EF 1(B)) from calf brain has been obtained by molecular sieve chromatography on Sephadex G-150. A high molecular weight form, EF 1(A), interacts with GTP to form an EF 1(A)-GTP complex. GDP also reacts with EF 1, but unlike the reaction with GTP, an EF 1(B)-GDP complex is formed that contains a lower molecular weight and labile specie...
متن کاملRecognition of the universally conserved 3'-CCA end of tRNA by elongation factor EF-Tu.
Escherichia coli tRNA(Val) with pyrimidine substitutions for the universally conserved 3'-terminal adenine can be readily aminoacylated. It cannot, however, transfer valine into polypeptides. Conversely, despite being a poor substrate for valyl-tRNA synthetase, tRNA(Val) with a 3'-terminal guanine is active in in vitro polypeptide synthesis. To better understand the function of the 3'-CCA seque...
متن کاملInhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.
Elongation factor G (EF G), bound to ribosomes either with GMPPCP or with fusidic acid and GDP, inhibits elongation factor Tu (EF Tu)-dependent binding of Phe-tRNA on the ribosome-poly(U) complex and binding of Ala-tRNA on the initiation complex formed with RNA from bacteriophage R17; GTP hydrolysis associated with Phe-tRNA binding is also inhibited. Moreover, nonenzymic binding of Phe-tRNA at ...
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...
متن کاملNucleotide 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.8.4545