Thiostrepton, an Inhibitor of 50 S Ribosome Subunit Function
نویسندگان
چکیده
منابع مشابه
Thiostrepton inhibition of tRNA delivery to the ribosome.
Ribosome-stimulated hydrolysis of guanosine-5'-triphosphate (GTP) by guanosine triphosphatase (GTPase) translation factors drives protein synthesis by the ribosome. Allosteric coupling of GTP hydrolysis by elongation factor Tu (EF-Tu) at the ribosomal GTPase center to messenger RNA (mRNA) codon:aminoacyl-transfer RNA (aa-tRNA) anticodon recognition at the ribosomal decoding site is essential fo...
متن کاملThe crystallization of ribosomal proteins from the 50 S subunit of the Escherichia coli and Bacillus stearothermophilus ribosome.
Several individual intact ribosomal proteins purified from bacterial sources under mild conditions have been crystallized. A number of these are suitable candidates for three-dimensional structural studies by x-ray diffraction techniques. Data collection to 3 A resolution for one of these proteins is in progress.
متن کاملTopography of RNA in the ribosome: location of the 3'-end of 5 S RNA on the central protuberance of the 50 S subunit.
The 5 S RNA is an integral part of the prokaryotic ribosome and plays an important role in polypeptide synthesis. However, the specific function of 5 S RNA and/or associated proteins is unknown” The removal of 5 S RNA from 50 S ribosomal subunits strongly impairs various functional activities of ribosomes [ 1,2]. The o&y exception is the EF-Gdependent GTP hydrolysis which is not influenced by t...
متن کاملStructure of the 80S Ribosome from Saccharomyces cerevisiae—tRNA-Ribosome and Subunit-Subunit Interactions
A cryo-EM reconstruction of the translating yeast 80S ribosome was analyzed. Computationally separated rRNA and protein densities were used for docking of appropriately modified rRNA models and homology models of yeast ribosomal proteins. The core of the ribosome shows a remarkable degree of conservation. However, some significant differences in functionally important regions and dramatic chang...
متن کاملThiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4
Thiostrepton, a macrocyclic thiopeptide antibiotic, inhibits prokaryotic translation by interfering with the function of elongation factor G (EF-G). Here, we have used 70S ribosome binding and GTP hydrolysis assays to study the effects of thiostrepton on EF-G and a newly described translation factor, elongation factor 4 (EF4). In the presence of thiostrepton, ribosome-dependent GTP hydrolysis i...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1970
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.101.3.1073-1075.1970