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The effect of tRNA binding on the structure of 5 S RNA in Escherichia coli. A chemical modification study.

Göringer, H. Ulrich ; Bertram, S. ; Wagner, R. :
The effect of tRNA binding on the structure of 5 S RNA in Escherichia coli. A chemical modification study.
In: The Journal of biological chemistry, 259 (1) pp. 491-6. ISSN 0021-9258
[Artikel], (1984)

Kurzbeschreibung (Abstract)

The structure of 5 S RNA within the 70 S ribosome from Escherichia coli was studied using the chemical reagent kethoxal (alpha-keto-beta-ethoxybutyraldehyde) to modify accessible guanosines. The modification pattern of 5 S RNA from free 70 S ribosomes was compared with that of poly(U) programmed ribosomes where tRNA had been bound to both the A- and P-sites. Binding to the ribosomal A-site was achieved enzymatically using the elongation factor Tu and GTP in the presence of deacylated tRNA which blocks the ribosomal P-site. Modified guanosines were identified after partial RNase T1 hydrolysis and separation of the hydrolysis products on sequencing gels. Binding of tRNA to the ribosome leads to a strong protection of 5 S RNA guanosine G-41 and to some degree G-44 from kethoxal modification. The limited RNase T1 hydrolysis pattern provides evidence for the existence of a 5 S RNA conformation different from the known 5 S RNA A- and B-forms which are characterized by their gel electrophoretic mobility. The importance of 5 S RNA for the binding of tRNA to the ribosome is discussed.

Typ des Eintrags: Artikel
Erschienen: 1984
Autor(en): Göringer, H. Ulrich ; Bertram, S. ; Wagner, R.
Titel: The effect of tRNA binding on the structure of 5 S RNA in Escherichia coli. A chemical modification study.
Sprache: Englisch
Kurzbeschreibung (Abstract):

The structure of 5 S RNA within the 70 S ribosome from Escherichia coli was studied using the chemical reagent kethoxal (alpha-keto-beta-ethoxybutyraldehyde) to modify accessible guanosines. The modification pattern of 5 S RNA from free 70 S ribosomes was compared with that of poly(U) programmed ribosomes where tRNA had been bound to both the A- and P-sites. Binding to the ribosomal A-site was achieved enzymatically using the elongation factor Tu and GTP in the presence of deacylated tRNA which blocks the ribosomal P-site. Modified guanosines were identified after partial RNase T1 hydrolysis and separation of the hydrolysis products on sequencing gels. Binding of tRNA to the ribosome leads to a strong protection of 5 S RNA guanosine G-41 and to some degree G-44 from kethoxal modification. The limited RNase T1 hydrolysis pattern provides evidence for the existence of a 5 S RNA conformation different from the known 5 S RNA A- and B-forms which are characterized by their gel electrophoretic mobility. The importance of 5 S RNA for the binding of tRNA to the ribosome is discussed.

Titel der Zeitschrift, Zeitung oder Schriftenreihe: The Journal of biological chemistry
Band: 259
(Heft-)Nummer: 1
Fachbereich(e)/-gebiet(e): Fachbereich Biologie, Biology > Genregulation und RNA-Therapeutika, Postranscriptional Gene Regulation and RNA Therapeutics
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Fachbereich Biologie, Biology
Hinterlegungsdatum: 07 Nov 2011 09:11
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