The elongin B ubiquitin homology domain

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dc.contributor.authorBrower, Christopher S.
dc.contributor.authorShilatifard, Ali
dc.contributor.authorMather, Timothy
dc.contributor.authorKamura, Takumi
dc.contributor.authorTakagi, Yuichiro
dc.contributor.authorHaque, Dewan
dc.contributor.authorTreharne, Annemarie
dc.contributor.authorFoundling, Stephen I.
dc.contributor.authorConaway, Joan Weliky
dc.contributor.authorConaway, Ronald C.
dc.creator.orcidhttps://orcid.org/0000-0003-0289-5541
dc.date.accessioned2023-01-27T18:48:35Z
dc.date.available2023-01-27T18:48:35Z
dc.date.issued1999
dc.description.abstractMammalian 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.en_US
dc.identifier.citationThis is the published version of an article that is available at https://doi.org/10.1074/jbc.274.19.13629. Recommended citation: Brower, C. S., Shilatifard, A., Mather, T., Kamura, T., Takagi, Y., Haque, D., Treharne, A., Foundling, S. I., Conaway, J. W., & Conaway, R. C. (1999). The elongin B ubiquitin homology domain. Journal of Biological Chemistry, 274(19), 13629–13636. This item has been deposited in accordance with publisher copyright and licensing terms and with the author’s permission.en_US
dc.identifier.urihttps://hdl.handle.net/11274/14348
dc.identifier.urihttps://doi.org/10.1074/jbc.274.19.13629
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.rights.licenseCC-BY 4.0
dc.subjectMultiprotein von Hippel-Lindau tumor suppressoren_US
dc.subjectCytokine signaling complexesen_US
dc.subjectSite-directed mutagenesisen_US
dc.titleThe elongin B ubiquitin homology domainen_US
dc.typeArticleen_US

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