Spontaneous, elongation factor G independent translocation of Escherichia coli ribosomes.
نویسندگان
چکیده
منابع مشابه
Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation.
During protein synthesis, elongation factor G (EF-G) binds to the ribosome and promotes the step of translocation, a process in which tRNA moves from the A to the P site of the ribosome and the mRNA is advanced by one codon. By using three-dimensional cryo-electron microscopy, we have visualized EF-G in a ribosome-EF-G-GDP-fusidic acid complex. Fitting the crystal structure of EF-G-GDP into the...
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The photoreactive guanosine triphosphate derivative PI(3-azido-6-hydroxymethylphenyl)-P3-(5’-guanosyl) triphosphate (azidosalicyl-GTP) was synthesized and characterized. In order to obtain this GTP derivative labeled with tritium with high specific activity, nonradioactive PI-(3azido-6-formylphenylj-P3-(5’-guanosyl) triphosphate was prepared. The aldehyde group of this compound was reduced with...
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Guanosine diphosphate esterified at the beta-phosphate group with the photolabile 4-azidophenol [1-(4-azidophenyl)-2-(5'-guanyl)pyrophosphate] was found to inhibit GDP binding to the ribosomes of E. coli. UV-irradiation of the fusidic acid-stabilized complex among ribosomes, elongation factor G, and the azidophenyl-GDP, results in selective attachment of the photo-affinity label to the proteins...
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The knowledge of the structure of the ribosome is an essential requirement to reveal its role at the molecular level in the process of protein biosynthesis. This information is being obtained by a battery of chemical, physical, immunological and genetic methods (for reviews see [1]). Important methods for the study of the three-dimensional structure of the ribosomes are X-ray crystallography an...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43778-1