Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain

Histone macroH2A1.2 (macroH2A) is an unusual histone H2A variant with a large non-histone macrodomain at its carboxyl terminal. MacroH2A1.2 is enriched in facultative heterochromatin, including inactivated X chromosomes in mammalian females and senescence-associated heterochromatin foci. We show her...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-10, Vol.336 (1), p.204-209
Main Authors: Ogawa, Y., Ono, T., Wakata, Y., Okawa, K., Tagami, H., Shibahara, K-i.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Blotting, Western
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Facultative heterochromatin
HeLa Cells
Histone macroH2A
Histone modification
Histone variants
Histones - chemistry
Histones - isolation & purification
Histones - metabolism
Humans
Molecular Sequence Data
Mono-ubiquitination
Nucleosomes - metabolism
Sequence Homology, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Ubiquitin - metabolism
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Summary:Histone macroH2A1.2 (macroH2A) is an unusual histone H2A variant with a large non-histone macrodomain at its carboxyl terminal. MacroH2A1.2 is enriched in facultative heterochromatin, including inactivated X chromosomes in mammalian females and senescence-associated heterochromatin foci. We show here that a small population of macroH2A1.2 is mono-ubiquitinated in human HeLa cells. Mass spectrometry analysis revealed that the specific targeting sites for the mono-ubiquitination are Lys115 and Lys116 of the histone domain. A corresponding Lys119 conserved in histone H2A is also mono-ubiquitinated by Ring protein in the polycomb group complex. We suggest that the mono-ubiquitination of macroH2A1.2 and histone H2A has similar or synergistic implications, but that the multiple ubiquitination sites in macroH2A1.2 might confer a variety of functions upon macroH2A1.2 to modulate chromatin states.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.08.046