Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP

Justin R Prigge; Edward E Schmidt

doi:10.1074/jbc.M510835200

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Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP

Journal article

Open access

Peer reviewed

Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP

Justin R Prigge and Edward E Schmidt

The Journal of biological chemistry, Vol.281(18), pp.12260-12269

05/05/2006

DOI: https://doi.org/10.1074/jbc.M510835200

Handle:

https://hdl.handle.net/2376/111576

PMCID: PMC2030495

PMID: 16522640

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Abstract

Amino Acid Sequence

Transcription Factors - chemistry

TATA-Box Binding Protein - physiology

Transcriptional Activation

Molecular Sequence Data

Male

Mice, Transgenic

Protein Inhibitors of Activated STAT - metabolism

Nuclear Proteins - chemistry

TATA-Box Binding Protein - metabolism

Sequence Homology, Amino Acid

Ubiquitin-Protein Ligases

Animals

Protein Inhibitors of Activated STAT - chemistry

Mice

Transcription activators often recruit promoter-targeted assembly of a pre-initiation complex; many repressors antagonize recruitment. These activities can involve direct interactions with proteins in the pre-initiation complex. We used an optimized yeast two-hybrid system to screen mouse pregnancy-associated libraries for proteins that interact with TATA-binding protein (TBP). Screens revealed an interaction between TBP and a single member of the zinc finger family of transcription factors, ZFP523. Two members of the protein inhibitor of activated STAT (PIAS) family, PIAS1 and PIAS3, also interacted with TBP in screens. Endogenous PIAS1 and TBP co-immunoprecipitated from nuclear extracts, suggesting the interaction occurred in vivo. In vitro-translated PIAS1 and TBP co-immunoprecipitated, which indicated that other nuclear proteins were not required for the interaction. Deletion analysis mapped the PIAS-interacting domain of TBP to the conserved TBP(CORE) and the TBP-interacting domain on PIAS1 to a 39-amino acid C-terminal region. Mammals issue seven known PIAS proteins from four pias genes, pias1, pias3, piasx, and piasy, each with different cell type-specific expression patterns; the TBP-interacting domain reported here is the only part of the PIAS C-terminal region shared by all seven PIAS proteins. Direct analyses indicated that PIASx and PIASy also interacted with TBP. Our results suggest that all PIAS proteins might mediate situation-specific regulatory signaling at the TBP interface and that previously unknown levels of complexity could exist in the gene regulatory interplay between TBP, PIAS proteins, ZFP523, and other transcription factors.

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Title: Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP
Creators: Justin R Prigge - Veterinary Molecular Biology, Montana State University, Bozeman, Montana 59717, USA
Edward E Schmidt
Publication Details: The Journal of biological chemistry, Vol.281(18), pp.12260-12269
Academic Unit: UNKNOWN
Publisher: United States
Grant note: R01 AI055739-03 / NIAID NIH HHS R01 AI055739-02 / NIAID NIH HHS R01 AI055739-01A1 / NIAID NIH HHS R01 AI055739 / NIAID NIH HHS R03 HD035824-02 / NICHD NIH HHS
Identifiers: 99900547693801842
Language: English
Resource Type: Journal article