TY - JOUR
T1 - Targeting activity is required for SWI/SNF function in vivo and is accomplished through two partially redundant activator-interaction domains
AU - Prochasson, Philippe
AU - Neely, Kristen E.
AU - Hassan, Ahmed H.
AU - Li, Bing
AU - Workman, Jerry L.
N1 - Funding Information:
We thank E.T. Young, B. Cairns, and B. Laurent for antisera against SWI/SNF subunits. A special thanks goes to Michael Carrozza for his help with the FPLC systems. Finally, we thank the members of the Workman, Simpson, Reese, and Tan labs at Penn State for valuable discussions. P.P. is a Postdoctoral Research Fellow of the Leukemia & Lymphoma Society, and J.L.W. is an Associate Investigator of the Howard Hughes Medical Institute. This work was supported by NIGMS grant R37 GM47867 to J.L.W.
PY - 2003/10
Y1 - 2003/10
N2 - The SWI/SNF complex is required for the expression of many yeast genes. Previous studies have implicated DNA binding transcription activators in targeting SWI/SNF to UASs and promoters. To determine how activators interact with the complex and to examine the importance of these interactions, relative to other potential targeting mechanisms, for SWI/SNF function, we sought to identify and mutate the activator-interaction domains in the complex. Here we show that the N-terminal domain of Snf5 and the second quarter of Swi1 are sites of activation domain contact. Deletion of both of these domains left the SWI/SNF complex intact but impaired its ability to bind activation domains. Importantly, while deletion of either domain alone had minor phenotypic effect, deletion of both resulted in strong SWI/SNF related phenotypes. Thus, two distinct activator-interaction domains play overlapping roles in the targeting activity of SWI/SNF, which is essential for its function in vivo.
AB - The SWI/SNF complex is required for the expression of many yeast genes. Previous studies have implicated DNA binding transcription activators in targeting SWI/SNF to UASs and promoters. To determine how activators interact with the complex and to examine the importance of these interactions, relative to other potential targeting mechanisms, for SWI/SNF function, we sought to identify and mutate the activator-interaction domains in the complex. Here we show that the N-terminal domain of Snf5 and the second quarter of Swi1 are sites of activation domain contact. Deletion of both of these domains left the SWI/SNF complex intact but impaired its ability to bind activation domains. Importantly, while deletion of either domain alone had minor phenotypic effect, deletion of both resulted in strong SWI/SNF related phenotypes. Thus, two distinct activator-interaction domains play overlapping roles in the targeting activity of SWI/SNF, which is essential for its function in vivo.
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U2 - 10.1016/S1097-2765(03)00366-6
DO - 10.1016/S1097-2765(03)00366-6
M3 - Article
C2 - 14580348
AN - SCOPUS:0242334110
SN - 1097-2765
VL - 12
SP - 983
EP - 990
JO - Molecular Cell
JF - Molecular Cell
IS - 4
ER -