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Direct binding of INHAT to H3 tails disrupted by modifications.
J. Biol. Chem. 279, 23859-23862 (2004)
The N-terminal tails of histones are central to the regulation of chromatin structure. They form a binding platform for multiple protein complexes, which in turn regulate DNA processes such as transcription. Using peptide mass fingerprinting we identified INHAT (inhibitor of acetyltransferases) as a specific histone H3 N-terminal tail-binding complex. INHAT comprises two essential subunits, SET and pp32. We demonstrate that both SET and pp32 bind directly to the N terminus of H3. The binding is differentially affected by various modifications within the H3 N terminus. In particular, single phosphorylations within the H3 tail abrogates binding of INHAT, as does the simultaneous acetylation of multiple lysine residues. The histone modifications that affect INHAT binding are therefore compatible with its known role in transcriptional repression. We suggest that the charge of the histone tail is a major determinant in allowing INHAT to bind chromatin and coordinate the activity of multiple histone acetyltransferases.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Sprache
englisch
Veröffentlichungsjahr
2004
HGF-Berichtsjahr
0
ISSN (print) / ISBN
0021-9258
e-ISSN
1083-351X
Zeitschrift
Journal of Biological Chemistry, The
Quellenangaben
Band: 279,
Heft: 23,
Seiten: 23859-23862
Verlag
American Society for Biochemistry and Molecular Biology
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Functional Epigenetics (IFE)
POF Topic(s)
30203 - Molecular Targets and Therapies
Forschungsfeld(er)
Helmholtz Diabetes Center
PSP-Element(e)
G-502800-001
PubMed ID
15100215
Erfassungsdatum
2004-12-31