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PMID: 9710597 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription.

Molecular and cellular biology ·Vol. 18 ·No. 9 ·1998-09-00 ·Pages 5128-39

Moilanen AM, Poukka H, Karvonen U, Häkli M, Jänne OA, Palvimo JJ

Abstract

Using the DNA-binding domain of androgen receptor (AR) as a bait in a yeast two-hybrid screening, we have identified a small nuclear RING finger protein, termed SNURF, that interacts with AR in a hormone-dependent fashion in both yeast and mammalian cells. Physical interaction between AR and SNURF was demonstrated by coimmunoprecipitation from cell extracts and by protein-protein affinity chromatography. Rat SNURF is a highly hydrophilic protein consisting of 194 amino acid residues and comprising a consensus C3HC4 zinc finger (RING) structure in the C-terminal region and a bipartite nuclear localization signal near the N terminus. Immunohistochemical experiments indicated that SNURF is a nuclear protein. SNURF mRNA is expressed in a variety of human and rat tissues. Overexpression of SNURF in cultured mammalian cells enhanced not only androgen, glucocorticoid, and progesterone receptor-dependent transactivation but also basal transcription from steroid-regulated promoters. Mutation of two of the potential Zn2+ coordinating cysteines to serines in the RING finger completely abolished the ability of SNURF to enhance basal transcription, whereas its ability to activate steroid receptor-dependent transcription was maintained, suggesting that there are separate domains in SNURF that mediate interactions with different regulatory factors. SNURF is capable of interacting in vitro with the TATA-binding protein, and the RING finger domain is needed for this interaction. Collectively, we have identified and characterized a ubiquitously expressed RING finger protein, SNURF, that may function as a bridging factor and regulate steroid receptor-dependent transcription by a mechanism different from those of previously identified coactivator or integrator proteins.

MeSH Terms
Amino Acid Sequence Animals CHO Cells COS Cells Cell Line Cloning, Molecular Cricetinae Gene Expression Regulation Gene Library HeLa Cells Humans Male Mice Molecular Sequence Data Nuclear Proteins/biosynthesis,chemistry,metabolism Rats Receptors, Androgen/metabolism Recombinant Fusion Proteins/biosynthesis,metabolism TATA Box Testis/metabolism Transcription Factors/biosynthesis,chemistry,metabolism Transcription, Genetic Transcriptional Activation Transfection Ubiquitin-Protein Ligases Zinc Fingers
Chemicals
Nuclear Proteins RNF4 protein, human Receptors, Androgen Recombinant Fusion Proteins Transcription Factors Rnf4 protein, mouse Rnf4 protein, rat Ubiquitin-Protein Ligases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Moilanen A M
Department of Physiology, Institute of Biomedicine, University of Helsinki, FIN-00014 Helsinki, Finland.
Poukka H
Karvonen U
Häkli M
Jänne O A
Palvimo J J
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.18.9.5128
Published
1998-09-00
Pages
5128-39
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC109098
Subset
IM
Databases
GENBANK
AF022081
External Links
PubMed source DOI: 10.1128/MCB.18.9.5128 PMC Full Text View journal details
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