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Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II
Author(s) -
Yang Jie,
Aittomäki Saara,
Pesu Marko,
Carter Kara,
Saarinen Jussi,
Kalkkinen Nisse,
Kieff Elliott,
Silvennoinen Olli
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdf463
Subject(s) - library science , university hospital , medicine , family medicine , computer science
STAT6 is a central mediator of IL‐4‐induced gene responses. STAT6‐mediated transcription is depend ent on the C‐terminal transcription activation domain (TAD), but the mechanisms by which STAT6 activates transcription are poorly understood. Here, we have identified the staphylococcal nuclease (SN)‐like domain and tudor domain containing protein p100 as a STAT6 TAD interacting protein. p100 was originally characterized as a transcriptional coactivator for Epstein–Barr virus nuclear antigen 2. STAT6 interacted with p100 in vitro and in vivo . The interaction was mediated by the TAD domain of STAT6 and the SN‐like domain of p100. p100 did not affect the immediate activation events of STAT6, but enhanced STAT6‐mediated transcriptional activation and the IL‐4‐induced Igϵ gene transcription in human B‐cell line. Finally, p100 associated with the large subunit of RNA polymerase II and was mediating interaction between STAT6 and RNA polymerase II. These findings identify p100 as a novel coactivator for STAT6 and suggest that p100 functions as a bridging factor between STAT6 and the basal transcription machinery.