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PMID: 2703476 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A protein-protein interaction is essential for stable complex formation on a 5 S RNA gene.

The Journal of biological chemistry ·Vol. 264 ·No. 11 ·1989-04-15 ·Pages 6009-12

Hayes J, Tullius TD, Wolffe AP

Abstract

Stable complex formation on a Xenopus somatic 5 S RNA gene requires protein-protein interactions between the non-DNA binding domain of transcription factor (TF) IIIA and activities in a TFIIIC fraction. No significant changes in the structure of the TFIIIA.DNA complex can be detected as a consequence of stabilization, indicating that protein confirmation is the primary determinant of stability.

MeSH Terms

Animals DNA, Ribosomal/metabolism DNA-Binding Proteins/metabolism Gene Expression Regulation Peptide Fragments/metabolism Protein Binding RNA, Ribosomal/genetics RNA, Ribosomal, 5S/genetics Regulatory Sequences, Nucleic Acid Structure-Activity Relationship Temperature Transcription Factors/metabolism Transcription, Genetic Xenopus laevis

Chemicals

DNA, Ribosomal DNA-Binding Proteins Peptide Fragments RNA, Ribosomal RNA, Ribosomal, 5S Transcription Factors

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Hayes J

Department of Chemistry, Johns Hopkins University, Baltimore, Maryland 21218.

Tullius T D

Wolffe A P

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1989-04-15

Pages

6009-12

Language

English

Region

United States

NLM ID

2985121R

Subset

Grants

PHS HHS · 01208 · United States

PHS HHS · 40894 · United States

External Links

PubMed source View journal details

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A protein-protein interaction is essential for stable complex formation on a 5 S RNA gene.

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