The Snf2 Homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme

Salma Awad; Daniel Ryan; Philippe Prochasson; Tom Owen-Hughes; Ahmed H. Hassan

doi:10.1074/jbc.M109.082149

The Snf2 Homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme

Salma Awad, Daniel Ryan, Philippe Prochasson, Tom Owen-Hughes, Ahmed H. Hassan

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Abstract

The Saccharomyces cerevisiae Fun30 (Function unknown now 30) protein shares homology with an extended family of Snf2-related ATPases. Here we report the purification of Fun30 principally as a homodimer with a molecular mass of about 250 kDa. Biochemical characterization of this complex reveals that it has ATPase activity stimulated by both DNA and chromatin. Consistent with this, it also binds to both DNA and chromatin. The Fun30 complex also exhibits activity in ATP-dependent chromatin remodeling assays. Interestingly, its activity in histone dimer exchange is high relative to the ability to reposition nucleosomes. Fun30 also possesses a weakly conserved CUE motif suggesting that it may interact specifically with ubiquitinylated proteins. However, in vitro Fun30 was found to have no specificity in its interaction with ubiquitinylated histones.

Original language	English
Pages (from-to)	9477-9484
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	285
Issue number	13
DOIs	https://doi.org/10.1074/jbc.M109.082149
Publication status	Published - 26 Mar 2010

Keywords

SACCHAROMYCES-CEREVISIAE
TRANSCRIPTIONAL REGULATOR
DNA TRANSLOCATION
PROTEIN COMPLEXES
CHROMOSOME-I
HISTONE
NUCLEOSOME
BINDING
GENES
IDENTIFICATION

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10.1074/jbc.M109.082149

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http://ukpmc.ac.uk/articles/PMC2843198

Cite this

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title = "The Snf2 Homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme",

abstract = "The Saccharomyces cerevisiae Fun30 (Function unknown now 30) protein shares homology with an extended family of Snf2-related ATPases. Here we report the purification of Fun30 principally as a homodimer with a molecular mass of about 250 kDa. Biochemical characterization of this complex reveals that it has ATPase activity stimulated by both DNA and chromatin. Consistent with this, it also binds to both DNA and chromatin. The Fun30 complex also exhibits activity in ATP-dependent chromatin remodeling assays. Interestingly, its activity in histone dimer exchange is high relative to the ability to reposition nucleosomes. Fun30 also possesses a weakly conserved CUE motif suggesting that it may interact specifically with ubiquitinylated proteins. However, in vitro Fun30 was found to have no specificity in its interaction with ubiquitinylated histones.",

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author = "Salma Awad and Daniel Ryan and Philippe Prochasson and Tom Owen-Hughes and Hassan, {Ahmed H.}",

year = "2010",

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language = "English",

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T1 - The Snf2 Homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme

AU - Awad, Salma

AU - Ryan, Daniel

AU - Prochasson, Philippe

AU - Owen-Hughes, Tom

AU - Hassan, Ahmed H.

PY - 2010/3/26

Y1 - 2010/3/26

N2 - The Saccharomyces cerevisiae Fun30 (Function unknown now 30) protein shares homology with an extended family of Snf2-related ATPases. Here we report the purification of Fun30 principally as a homodimer with a molecular mass of about 250 kDa. Biochemical characterization of this complex reveals that it has ATPase activity stimulated by both DNA and chromatin. Consistent with this, it also binds to both DNA and chromatin. The Fun30 complex also exhibits activity in ATP-dependent chromatin remodeling assays. Interestingly, its activity in histone dimer exchange is high relative to the ability to reposition nucleosomes. Fun30 also possesses a weakly conserved CUE motif suggesting that it may interact specifically with ubiquitinylated proteins. However, in vitro Fun30 was found to have no specificity in its interaction with ubiquitinylated histones.

AB - The Saccharomyces cerevisiae Fun30 (Function unknown now 30) protein shares homology with an extended family of Snf2-related ATPases. Here we report the purification of Fun30 principally as a homodimer with a molecular mass of about 250 kDa. Biochemical characterization of this complex reveals that it has ATPase activity stimulated by both DNA and chromatin. Consistent with this, it also binds to both DNA and chromatin. The Fun30 complex also exhibits activity in ATP-dependent chromatin remodeling assays. Interestingly, its activity in histone dimer exchange is high relative to the ability to reposition nucleosomes. Fun30 also possesses a weakly conserved CUE motif suggesting that it may interact specifically with ubiquitinylated proteins. However, in vitro Fun30 was found to have no specificity in its interaction with ubiquitinylated histones.

KW - SACCHAROMYCES-CEREVISIAE

KW - TRANSCRIPTIONAL REGULATOR

KW - DNA TRANSLOCATION

KW - PROTEIN COMPLEXES

KW - CHROMOSOME-I

KW - HISTONE

KW - NUCLEOSOME

KW - BINDING

KW - GENES

KW - IDENTIFICATION

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DO - 10.1074/jbc.M109.082149

M3 - Article

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SN - 0021-9258

VL - 285

SP - 9477

EP - 9484

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 13

ER -

The Snf2 Homolog Fun30 acts as a homodimeric ATP-dependent chromatin-remodeling enzyme

Abstract

Keywords

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