Transcription activator interactions with multiple SWI/SNF subunits.
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.
Neely
Kristen E
KE
Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, The Pennsylvania State University, University Park, PA 16802, USA.
Hassan
Ahmed H
AH
Brown
Christine E
CE
Howe
LeAnn
L
Workman
Jerry L
JL
D000143:Acids / Q000378:metabolism; D000251:Adenosine Triphosphatases; D023081:CCAAT-Binding Factor / Q000378:metabolism; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D003432:Cross-Linking Reagents / Q000737:chemistry / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D010777:Photochemistry; D011485:Protein Binding / Q000187:drug effects / Q000502:physiology; D011494:Protein Kinases / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D000071796:SMARCB1 Protein; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D015533:Transcriptional Activation / Q000502:physiology*
D000143:Acids; D023081:CCAAT-Binding Factor; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D003432:Cross-Linking Reagents; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C061437:HAP4 protein, S cerevisiae; D046911:Macromolecular Substances; D009687:Nuclear Proteins; C060292:PHO4 protein, S cerevisiae; D021122:Protein Subunits; D011994:Recombinant Proteins; D000071796:SMARCB1 Protein; C513266:SMARCB1 protein, human; C066190:SNF5 protein, S cerevisiae; C078562:SWI1 protein, S cerevisiae; C080218:SWI5 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011494:Protein Kinases; C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases; D000251:Adenosine Triphosphatases; C499333:SNF2 protein, S cerevisiae