A Specific Ribonucleoprotein Fragment from Escherichia coli 30-S Ribosomes. Location of the RNA Component in 16-S RNA
نویسندگان
چکیده
منابع مشابه
A ribonucleoprotein fragment of the 30 S ribosome of E. coli: evidence for long range RNA-RNA interactions.
A stable homogeneous ribonucleoprotein fragment of the 30 S ribosomal subunit of E. coli has been prepared by mild nuclease digestion and heating in a constant ionic environment. The fragment contains about half of the 16 S ribosomal RNa and six proteins: S4, S7, S9, S13, S16 and S19. The RNA moiety contains the reported binding sites of all six proteins. After deproteinization, 80% of the RNA ...
متن کاملThe hydrodynamic and spectroscopic properties of 16 S RNA from Escherichia coli ribosome in reconstitution buffer.
The hydrodynamic shape, conformation, and thermal stability of ribosomal16 S RNA in reconstitution buffer have been studied by sedimentation velocity, intrinsic viscosity, circular dichroism, and difference ultraviolet absorption spectroscopy. These results are compared with the corresponding properties of the 30 S ribosomal subunit in order to understand the role of the RNA molecule in the ass...
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An RNA-protein complex was isolated from the 50S subunit of E. coli ribosomes after trypsin digestion. The complex contains only one protein, L24. Treatment of the complex with pancreatic ribonuclease results in digestion of most of the RNA; however, an RNA fragment of about 100 nucleotides in length is stable to nuclease digestion and remains bound to the protein. It is also possible to recons...
متن کاملStudies and sequences of Escherichia coli 4.5 S RNA.
4.5 S RNA, a biologically stable species with electrophoretic properties intermediate between 5 S and transfer RNAs, has been isolated from Escherichia coli and characterized. No function has yet been found for this molecule. Its primary structure and behavior suggests an unusually stable and possibly unique secondary structure. Even from single species of E. coli, there is some sequence het...
متن کاملCharacterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli.
An Escherichia coli open reading frame, ygcA, was identified as a putative 23 S ribosomal RNA 5-methyluridine methyltransferase (Gustafsson, C., Reid, R., Greene, P. J., and Santi, D. V. (1996) Nucleic Acids Res. 24, 3756-3762). We have cloned, expressed, and purified the 50-kDa protein encoded by ygcA. The purified enzyme catalyzed the AdoMet-dependent methylation of 23 S rRNA but did not act ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1973
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1973.tb02875.x