Literature DB >> 20493169

Histone acetylation facilitates association of nucleosomes with SET domain of ALL-1 methyltransferase in vitro.

Wladyslaw A Krajewski1, Oleg L Vassiliev.   

Abstract

The inheritable methylation pattern of gene activity, created upon cell differentiation, is further maintained by the "SET" (methyltransferase)-domain proteins. However, it is still not clear how SET-proteins can decide on the required gene activity state and the way their chromatin association is maintained. Here we have found that high levels of histone acetylation--the hallmarks of active chromosome regions in vivo--can increase the affinity of reconstituted nucleosomes to the SET domain of ALL-1 histone methyltransferase in a defined system in vitro. Copyright (c) 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20493169     DOI: 10.1016/j.bbrc.2010.05.080

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex.

Authors:  Anamika Patel; Valarie E Vought; Venkatasubramanian Dharmarajan; Michael S Cosgrove
Journal:  J Biol Chem       Date:  2010-11-24       Impact factor: 5.157

2.  Interaction of SET domains with histones and nucleic acid structures in active chromatin.

Authors:  Wladyslaw A Krajewski; Oleg L Vassiliev
Journal:  Clin Epigenetics       Date:  2011-01-14       Impact factor: 6.551

3.  The chromatin remodeler ISWI regulates the cellular response to hypoxia: role of FIH.

Authors:  Andrew Melvin; Sharon Mudie; Sonia Rocha
Journal:  Mol Biol Cell       Date:  2011-09-07       Impact factor: 4.138

  3 in total

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