The Elongin B ubiquitin homology domain. Identification of Elongin B sequences important for interaction with Elongin C

Christopher S. Brower, Ali Shilatifard, Timothy Mather, Takumi Kamura, Yuichiro Takagi, Dewan Haque, Annemarie Treharne, Stephen I. Foundling, Joan Weliky Conaway, Ronald C. Conaway

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Mammalian Elongin B is a 118-amino acid protein composed of an 84-amino acid amino-terminal ubiquitin-like domain and a 34-amino acid carboxyl- terminal tail. Elongin B is found in cells as a subunit of the heterodimeric Elongin BC complex, which was originally identified as a positive regulator of RNA polymerase II elongation factor Elongin A and subsequently as a component of the multiprotein von Hippel-Lindau tumor suppressor and suppressor of cytokine signaling complexes. As part of our effort to understand how the Elongin BC complex regulates the activity of Elongin A, we are characterizing Elongin B functional domains. In this report, we show that the Elongin B ubiquitin-like domain is necessary and sufficient for interaction with Elongin C and for positive regulation of Elongin A transcriptional activity. In addition, by site-directed mutagenesis of the Elongin B ubiquitin-like domain, we identify a short Elongin B region that is important for its interaction with Elongin C. Finally, we observe that both the ubiquitin-like domain and carboxyl-terminal tail are conserved in Drosophila melanogaster and Caenorhabditis elegans Elongin B homologs that efficiently substitute for mammalian Elongin B in reconstitution of the transcriptionally active Elongin ABC complex, suggesting that the carboxyl- terminal tail performs an additional function not detected in our assays.

Original languageEnglish (US)
Pages (from-to)13629-13636
Number of pages8
JournalJournal of Biological Chemistry
Volume274
Issue number19
DOIs
StatePublished - May 7 1999
Externally publishedYes

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Ubiquitin
Tail
elongin
Amino Acids
Peptide Elongation Factors
Mutagenesis
RNA Polymerase II
Caenorhabditis elegans
Site-Directed Mutagenesis
Drosophila melanogaster
Tumors
Assays

ASJC Scopus subject areas

  • Biochemistry

Cite this

The Elongin B ubiquitin homology domain. Identification of Elongin B sequences important for interaction with Elongin C. / Brower, Christopher S.; Shilatifard, Ali; Mather, Timothy; Kamura, Takumi; Takagi, Yuichiro; Haque, Dewan; Treharne, Annemarie; Foundling, Stephen I.; Conaway, Joan Weliky; Conaway, Ronald C.

In: Journal of Biological Chemistry, Vol. 274, No. 19, 07.05.1999, p. 13629-13636.

Research output: Contribution to journalArticle

Brower, CS, Shilatifard, A, Mather, T, Kamura, T, Takagi, Y, Haque, D, Treharne, A, Foundling, SI, Conaway, JW & Conaway, RC 1999, 'The Elongin B ubiquitin homology domain. Identification of Elongin B sequences important for interaction with Elongin C', Journal of Biological Chemistry, vol. 274, no. 19, pp. 13629-13636. https://doi.org/10.1074/jbc.274.19.13629
Brower, Christopher S. ; Shilatifard, Ali ; Mather, Timothy ; Kamura, Takumi ; Takagi, Yuichiro ; Haque, Dewan ; Treharne, Annemarie ; Foundling, Stephen I. ; Conaway, Joan Weliky ; Conaway, Ronald C. / The Elongin B ubiquitin homology domain. Identification of Elongin B sequences important for interaction with Elongin C. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 19. pp. 13629-13636.
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