Physical association of the APIS complex and general transcription factors

被引:43
作者
Sun, LP
Johnston, SA
Kodadek, T
机构
[1] Univ Texas, SW Med Ctr, Dept Internal Med, Dallas, TX 75390 USA
[2] Univ Texas, SW Med Ctr, Dept Biol Mol, Dallas, TX 75390 USA
关键词
D O I
10.1016/S0006-291X(02)02026-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It has recently been demonstrated that a fragment of the proteasome, called the APIS complex, plays an important role in RNA polymerase II-mediated transcription. Here, it is shown that the APIS complex is physically associated with many general transcription factors, including components of yeast FACT (Cdc68/Pob3), TFIID, TFIIH, and the RNA polymerase II holoenzyme. Depletion of this APIS/transcription factor complex from a yeast whole cell extract resulted in reduced transcription, indicating that it is functionally relevant. The APIS/transcription factor complex does not include detectable levels of the 20S proteolytic sub-unit of the proteasome. Furthermore, immunopurified 26S proteasome contains little or no transcription factors, suggesting that transcription factors and the 20S bind competitively to the APIS complex. These data add to the growing body of evidence that the ARIS complex has a role in transcription, independent of its role in proteolysis and, furthermore, argues that it functions in association with the general transcription complex. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:991 / 999
页数:9
相关论文
共 54 条
[1]   HBV X protein targets HIV tat-binding protein 1 [J].
Barak, O ;
Aronheim, A ;
Shaul, Y .
VIROLOGY, 2001, 283 (01) :110-120
[2]   The proteasome:: Paradigm of a self-compartmentalizing protease [J].
Baumeister, W ;
Walz, J ;
Zühl, F ;
Seemuller, E .
CELL, 1998, 92 (03) :367-380
[3]   The base of the proteasome regulatory particle exhibits chaperone-like activity [J].
Braun, BC ;
Glickman, M ;
Kraft, R ;
Dahlmann, B ;
Kloetzel, PM ;
Finley, D ;
Schmidt, M .
NATURE CELL BIOLOGY, 1999, 1 (04) :221-226
[4]   Biochemistry and structural biology of transcription factor IID (TFIID) [J].
Burley, SK ;
Roeder, RG .
ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :769-799
[5]   The Gal4 activation domain binds Sug2 protein, a proteasome component, in vivo and in vitro [J].
Chang, C ;
Gonzalez, F ;
Rothermel, B ;
Sun, LP ;
Johnston, SA ;
Kodadek, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (33) :30956-30963
[6]   Control of elongation by RNA polymerase II [J].
Conaway, JW ;
Shilatifard, A ;
Dvir, A ;
Conaway, RC .
TRENDS IN BIOCHEMICAL SCIENCES, 2000, 25 (08) :375-380
[7]   Structure and functions of the 20S and 26S proteasomes [J].
Coux, O ;
Tanaka, K ;
Goldberg, AL .
ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 :801-847
[8]   6-AZAURACIL INHIBITION OF GTP BIOSYNTHESIS IN SACCHAROMYCES-CEREVISIAE [J].
EXINGER, F ;
LACROUTE, F .
CURRENT GENETICS, 1992, 22 (01) :9-11
[9]   The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II [J].
Ferdous, A ;
Gonzalez, F ;
Sun, LP ;
Kodadek, T ;
Johnston, SA .
MOLECULAR CELL, 2001, 7 (05) :981-991
[10]   The 19S complex of the proteasome regulates nucleotide excision repair in yeast [J].
Gillette, TG ;
Huang, W ;
Russell, SJ ;
Reed, SH ;
Johnston, SA ;
Friedberg, EC .
GENES & DEVELOPMENT, 2001, 15 (12) :1528-1539