Characterization of elongin C functional domains required for interaction with Elongin B and activation of Elongin A

Yuichiro Takagi, Ronald C. Conaway, Joan Weliky Conaway

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The Elongin (SIII) complex stimulates the rate of elongation by RNA polymerase II by suppressing transient pausing by polymerase at many sites along DNA templates. The Elongin (SIII) complex is composed of a transcriptionally active A subunit, a chaperone-like B subunit, which promotes assembly and enhances stability of the Elongin (SIII) complex, and a regulatory C subunit, which (i) functions as a potent activator of Elongin A transcriptional activity, (ii) interacts specifically with Elongin B to form an isolable Elongin BC complex, and (iii) is bound and negatively regulated in vitro by the product of the von Hippel-Lindau tumor suppressor gene. As part of our effort to understand how Elongin C regulates the activity of the Elongin (SIII) complex, we are characterizing Elongin C functional domains. In this report, we identify Elongin C mutants that fall into multiple functional classes based on their abilities to bind Elongin B and to bind and activate Elongin A under our assay conditions. Characterization of these mutants suggests that Elongin C is composed of multiple overlapping regions that mediate functional interactions with Elongin A and B.

Original languageEnglish (US)
Pages (from-to)25562-25568
Number of pages7
JournalJournal of Biological Chemistry
Volume271
Issue number41
DOIs
StatePublished - 1996
Externally publishedYes

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Chemical activation
elongin
RNA Polymerase II
Tumor Suppressor Genes
Tumors
Elongation
Assays
Genes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characterization of elongin C functional domains required for interaction with Elongin B and activation of Elongin A. / Takagi, Yuichiro; Conaway, Ronald C.; Conaway, Joan Weliky.

In: Journal of Biological Chemistry, Vol. 271, No. 41, 1996, p. 25562-25568.

Research output: Contribution to journalArticle

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