Interactions of Guanosine Triphosphate Analogues with Elongation Factor G of Escherichia coli
نویسندگان
چکیده
منابع مشابه
Preparation of homogeneous elongation factor G and examination of the mechanism of guanosine triphosphate hydrolysis.
A new procedure for the isolation of physically and enzymatically homogeneous Elongation Factor G based on the isolation of an Elongation Factor G. ribosome . GDP. fusidic acid complex is described. The yield from this procedure is 23 to 36% of the theoretical and results in an enzyme of specific activity 6200 to 6700 units per AyaO. The enzyme was shown to be physically homogeneous by disc gel...
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The role of GTP in the translocation reaction catalyzed by elongation factor G (EF-G) has been investigated. The addition of EF-G and GTP to a poly(U)-ribosome complex having deacylated tRNA in the P site and N-acetykliphenylalanyl-tRNA in the A site (Complex II) results in the shift of N-acetyldiphenylalanyl-tRNA from the A to the P site of ribosomes with a concomitant release of tRNA from the...
متن کاملRole of guanine nucleotides in protein synthesis. Elongation factor G and guanosine 5'-triphosphate,3'-diphosphate.
The possible role of guanosine 5'-triphosphate,3'-diphosphate (pppGpp) in protein synthesis by Escherichia coli ribosomes and protein factors was examined. Although pppGpp could effectively substitute for GTP in reactions catalyzed by initiation factor 2 (ribosomal binding of fMet-tRNA and formation of N-formylmethionylpuromycin) and elongation factor T (ribosomal binding of Phe-tRNA and format...
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The interaction of protein synthesis elongation factor 1 (EF-1) from wheat embryos and elongation factor Tu from Escherichia coli with cytidylyl(5’-3’)guanosine 5’-triphosphate(pppGpC) has been studied. The dinucleotide 5’-triphosphate interacts strongly with EF-1 as evidenced by its capacity to inhibit the binding of [3H]GTP to the factor. The analogs pGpC and GpC do not interfere with GTP bin...
متن کاملVisualization 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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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1976
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1976.tb10245.x