PRC2 and SWI/SNF Chromatin Remodeling Complexes in Health and Disease

The dynamic structure of histones and DNA, also known as chromatin, is regulated by two classes of enzymes: those that mediate covalent modifications on either histone proteins or DNA and those that use the energy generated by ATP hydrolysis to mechanically alter chromatic structure. Both classes of...

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Bibliographic Details
Published in:Biochemistry (Easton) 2016-03, Vol.55 (11), p.1600-1614
Main Authors: Kadoch, Cigall, Copeland, Robert A, Keilhack, Heike
Format: Article
Language:English
Subjects:
Animals
Chromatin Assembly and Disassembly
Chromosomal Proteins, Non-Histone - metabolism
DNA, Neoplasm - metabolism
Enhancer of Zeste Homolog 2 Protein
Heterochromatin - metabolism
Heterochromatin - pathology
Histones - metabolism
Humans
Neoplasm Proteins - metabolism
Neoplasm Proteins - pharmacology
Neoplasms - metabolism
Neoplasms - pathology
Polycomb Repressive Complex 2 - metabolism
Protein Processing, Post-Translational
Transcription Factors - metabolism
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Summary:The dynamic structure of histones and DNA, also known as chromatin, is regulated by two classes of enzymes: those that mediate covalent modifications on either histone proteins or DNA and those that use the energy generated by ATP hydrolysis to mechanically alter chromatic structure. Both classes of enzymes are often found in large protein complexes. In this review, we describe two such complexes: polycomb repressive complex 2 (PRC2), with the protein methyltransferase EZH2 as its catalytic subunit, and the ATP-dependent chromatin remodeler switch/sucrose non-fermentable (SWI/SNF). EZH2 catalyzes the methylation of lysine 27 on histone H3, a covalent chromatin modification that is associated with repressed heterochromatin. The catalytic activity of SWI/SNF, in contrast, leads to a state of open chromatin associated with active transcription. In this review, we discuss the biochemical properties of both complexes, outline the principles of their regulation, and describe their opposing roles in normal development, which can be perturbed in disease settings such as cancer.
ISSN:0006-2960
1520-4995
DOI:10.1021/acs.biochem.5b01191