Studies on the RNA and protein binding sites of the E. coli ribosomal protein L10.

Nucleic acids research ·Vol. 6 ·No. 7 ·1979-06-11 ·Pages 2637-46

Pettersson I

Abstract

We have used modification of specific amino acid residues in the E. coli ribosomal protein L10 as a tool to study its interactions with another ribosomal protein, L7/L12, as well as with ribosomal core particles and with 23S RNA. The ribosome and RNA binding capability of L10 was found to be inhibited by modification of one more of its arginine residues. This treatment does not affect the ability of L10 to bind four molecules of L7/L12 in a L7/L12-L10 complex. Our results support the view that L10's role in promoting the L7/L12-ribosome association is due primarily to its ability to bind to both 23S RNA and L7/L12 simultaneously.

MeSH Terms

Amino Acids Binding Sites Diacetyl Escherichia coli/metabolism Kinetics Protein Binding RNA, Ribosomal/metabolism Ribosomal Proteins/metabolism Ribosomes/metabolism

Chemicals

Amino Acids RNA, Ribosomal Ribosomal Proteins Diacetyl

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Pettersson I

References (23)

23 references, click to expand

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Article Info

Journal

Nucleic acids research

Abbr.

Nucleic Acids Res

ISSN

0305-1048

DOI

10.1093/nar/6.7.2637

Published

1979-06-11

Pages

2637-46

Language

English

Region

England

NLM ID

0411011

PMCID

PMC327877

Subset

External Links

PubMed source DOI: 10.1093/nar/6.7.2637 PMC Full Text View journal details

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Studies on the RNA and protein binding sites of the E. coli ribosomal protein L10.

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