TY - JOUR
T1 - Transcription activator interactions with multiple SWI/SNF subunits
AU - Neely, Kristen E.
AU - Hassan, Ahmed H.
AU - Brown, Christine E.
AU - Howe, Le Ann
AU - Workman, Jerry L.
PY - 2002/3/1
Y1 - 2002/3/1
N2 - We have previously shown that the yeast SWI/SNF complex stimulates in vitro transcription from chromatin templates in an ATP-dependent manner. SWI/SNF function in this regard requires the presence of an activator with which it can interact directly, linking activator recruitment of SWI/SNF to transcriptional stimulation. In this study, we determine the SWI/SNF subunits that mediate its interaction with activators. Using a photo-cross-linking label transfer strategy, we show that the Snf5, Swi1, and Swi2/Snf2 subunits are contacted by the yeast acidic activators, Gcn4 and Hap4, in the context of the intact native SWI/SNF complex. In addition, we show that the same three subunits can interact individually with acidic activation domains, indicating that each subunit contributes to binding activators. Furthermore, mutations that reduce the activation potential of these activators also diminish its interaction with each of these SWI/SNF subunits. Thus, three distinct subunits of the SWI/SNF complex contribute to its interactions with activation domains.
AB - We have previously shown that the yeast SWI/SNF complex stimulates in vitro transcription from chromatin templates in an ATP-dependent manner. SWI/SNF function in this regard requires the presence of an activator with which it can interact directly, linking activator recruitment of SWI/SNF to transcriptional stimulation. In this study, we determine the SWI/SNF subunits that mediate its interaction with activators. Using a photo-cross-linking label transfer strategy, we show that the Snf5, Swi1, and Swi2/Snf2 subunits are contacted by the yeast acidic activators, Gcn4 and Hap4, in the context of the intact native SWI/SNF complex. In addition, we show that the same three subunits can interact individually with acidic activation domains, indicating that each subunit contributes to binding activators. Furthermore, mutations that reduce the activation potential of these activators also diminish its interaction with each of these SWI/SNF subunits. Thus, three distinct subunits of the SWI/SNF complex contribute to its interactions with activation domains.
UR - http://www.scopus.com/inward/record.url?scp=0036176172&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036176172&partnerID=8YFLogxK
U2 - 10.1128/MCB.22.6.1615-1625.2002
DO - 10.1128/MCB.22.6.1615-1625.2002
M3 - Article
C2 - 11865042
AN - SCOPUS:0036176172
SN - 0270-7306
VL - 22
SP - 1615
EP - 1625
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
IS - 6
ER -