Highly acidic C-terminal domain of pp32 is required for the interaction with histone chaperone, TAF-Ibeta.

Abstract:

:We have previously reported that INHAT (inhibitor of acetyltransferases) complex subunits, TAF (template activating factor)-Ialpha, TAF-Ibeta and pp32 can inhibit histone acetylation and HAT (histone acetyltransferase)-dependent transcription by binding to histones. Evidences are accumulating that INHAT complex subunits have important regulatory roles in various cellular activities such as replication, transcription, and apoptosis etc. However, how these subunits interact each other remains largely unknown. Using immunoprecipitation (IP) and protein-protein interaction assays with TAF-Ibeta and pp32 deletion mutant proteins, we identify INHAT complex subunits, TAF-Ibeta and pp32 interaction requires highly acidic C-terminal domain of pp32. We also show that the interaction between the INHAT complex subunits is stronger in the presence of histones. In this study, we report that the synergistic inhibition of HAT-mediated transcription by TAF-Ibeta and pp32 is dependent on the highly acidic C-terminal domain of pp32.

journal_name

Biol Pharm Bull

authors

Lee IS,Oh SM,Kim SM,Lee DS,Seo SB

doi

10.1248/bpb.29.2395

subject

Has Abstract

pub_date

2006-12-01 00:00:00

pages

2395-8

issue

12

eissn

0918-6158

issn

1347-5215

pii

JST.JSTAGE/bpb/29.2395

journal_volume

29

pub_type

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