Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes

Laurie A. Boyer; Michael R. Langer; Kimberly A. Crowley; Song Tan; John M. Denu; Craig L. Peterson

doi:10.1016/S1097-2765(02)00634-2

Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes

Laurie A. Boyer, Michael R. Langer, Kimberly A. Crowley, Song Tan, John M. Denu, Craig L. Peterson

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208 Scopus citations

Abstract

The SANT domain is a novel motif found in a number of eukaryotic transcriptional regulatory proteins that was identified based on its homology to the DNA binding domain of c-myb. Here we show that the SANT domain is essential for the in vivo functions of yeast Swi3p, Ada2p, and Rsc8p, subunits of three distinct chromatin remodeling complexes. We also find that the Ada2p SANT domain is essential for histone acetyltransferase activity of native, Gcn5p-containing HAT complexes. Furthermore, kinetic analyses indicate that an intact SANT domain is required for an Ada2p-dependent enhancement of histone tail binding and enzymatic catalysis by Gcn5p. Our results are consistent with a general role for SANT domains in functional interactions with histone N-terminal tails.

Original language	English (US)
Pages (from-to)	935-942
Number of pages	8
Journal	Molecular cell
Volume	10
Issue number	4
DOIs	https://doi.org/10.1016/S1097-2765(02)00634-2
State	Published - Oct 1 2002

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1016/S1097-2765(02)00634-2

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title = "Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes",

abstract = "The SANT domain is a novel motif found in a number of eukaryotic transcriptional regulatory proteins that was identified based on its homology to the DNA binding domain of c-myb. Here we show that the SANT domain is essential for the in vivo functions of yeast Swi3p, Ada2p, and Rsc8p, subunits of three distinct chromatin remodeling complexes. We also find that the Ada2p SANT domain is essential for histone acetyltransferase activity of native, Gcn5p-containing HAT complexes. Furthermore, kinetic analyses indicate that an intact SANT domain is required for an Ada2p-dependent enhancement of histone tail binding and enzymatic catalysis by Gcn5p. Our results are consistent with a general role for SANT domains in functional interactions with histone N-terminal tails.",

author = "Boyer, {Laurie A.} and Langer, {Michael R.} and Crowley, {Kimberly A.} and Song Tan and Denu, {John M.} and Peterson, {Craig L.}",

note = "Funding Information: We wish to thank M. Carlson for providing the RSC8 strains and plasmids and F. Winston, S. Berger, and M. Green for antibodies. This work was supported by grants from the NIH to C.L.P (GM49650) and S.T. (GM60489) and from the NIH (GM59785) and American Cancer Society (RSG-01-029-01-CNE) to J.M.D.",

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doi = "10.1016/S1097-2765(02)00634-2",

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T1 - Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes

AU - Boyer, Laurie A.

AU - Langer, Michael R.

AU - Crowley, Kimberly A.

AU - Tan, Song

AU - Denu, John M.

AU - Peterson, Craig L.

N1 - Funding Information: We wish to thank M. Carlson for providing the RSC8 strains and plasmids and F. Winston, S. Berger, and M. Green for antibodies. This work was supported by grants from the NIH to C.L.P (GM49650) and S.T. (GM60489) and from the NIH (GM59785) and American Cancer Society (RSG-01-029-01-CNE) to J.M.D.

PY - 2002/10/1

Y1 - 2002/10/1

N2 - The SANT domain is a novel motif found in a number of eukaryotic transcriptional regulatory proteins that was identified based on its homology to the DNA binding domain of c-myb. Here we show that the SANT domain is essential for the in vivo functions of yeast Swi3p, Ada2p, and Rsc8p, subunits of three distinct chromatin remodeling complexes. We also find that the Ada2p SANT domain is essential for histone acetyltransferase activity of native, Gcn5p-containing HAT complexes. Furthermore, kinetic analyses indicate that an intact SANT domain is required for an Ada2p-dependent enhancement of histone tail binding and enzymatic catalysis by Gcn5p. Our results are consistent with a general role for SANT domains in functional interactions with histone N-terminal tails.

AB - The SANT domain is a novel motif found in a number of eukaryotic transcriptional regulatory proteins that was identified based on its homology to the DNA binding domain of c-myb. Here we show that the SANT domain is essential for the in vivo functions of yeast Swi3p, Ada2p, and Rsc8p, subunits of three distinct chromatin remodeling complexes. We also find that the Ada2p SANT domain is essential for histone acetyltransferase activity of native, Gcn5p-containing HAT complexes. Furthermore, kinetic analyses indicate that an intact SANT domain is required for an Ada2p-dependent enhancement of histone tail binding and enzymatic catalysis by Gcn5p. Our results are consistent with a general role for SANT domains in functional interactions with histone N-terminal tails.

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JO - Molecular cell

JF - Molecular cell

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Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes

Abstract

All Science Journal Classification (ASJC) codes

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