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Molecular and Cellular Biology, December 2002, p. 8774-8786, Vol. 22, No. 24
0270-7306/02/$04.00+0 DOI: 10.1128/MCB.22.24.8774-8786.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
The Novel SLIK Histone Acetyltransferase Complex Functions in the Yeast Retrograde Response Pathway
Marilyn G. Pray-Grant,1 David Schieltz,2 Stacey J. McMahon,1 Jennifer M. Wood,1 Erin L. Kennedy,1 Richard G. Cook,3 Jerry L. Workman,4 John R. Yates III,5 and Patrick A. Grant1*
Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia 22908,1
Torrey Mesa Research Institute, San Diego, California 92121,2
Department of Immunology, Baylor College of Medicine, Houston, Texas 77030,3
Howard Hughes Medical Institute and the Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802,4
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 920375
Received 25 June 2002/
Returned for modification 19 August 2002/
Accepted 19 September 2002
The SAGA complex is a conserved histone acetyltransferase-coactivator that regulates gene expression in Saccharomyces cerevisiae. SAGA contains a number of subunits known to function in transcription including Spt and Ada proteins, the Gcn5 acetyltransferase, a subset of TATA-binding-protein-associated factors (TAFIIs), and Tra1. Here we report the identification of SLIK (SAGA-like), a complex related in composition to SAGA. Notably SLIK uniquely contains the protein Rtg2, linking the function of SLIK to the retrograde response pathway. Yeast harboring mutations in both SAGA and SLIK complexes displays synthetic phenotypes more severe than those of yeast with mutation of either complex alone. We present data indicating that distinct forms of the SAGA complex may regulate specific subsets of genes and that SAGA and SLIK have multiple partly overlapping activities, which play a critical role in transcription by RNA polymerase II.
* Corresponding author. Mailing address: University of Virginia Health System, Box 800733, Charlottesville, VA 22908. Phone: (434) 243-5766. Fax: (434) 924-5069. E-mail:
pag9n{at}virginia.edu.
Molecular and Cellular Biology, December 2002, p. 8774-8786, Vol. 22, No. 24
0022-538X/02/$04.00+0 DOI: 10.1128/MCB.22.24.8774-8786.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
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