Differential underacetylation of histones H2A, H3 and H4 on the inactive X chromosome in human female cells.
It has previously been shown that the acetylated forms of histone H4 are depleted or absent in both constitutive, centric heterochromatin and in the facultative heterochromatin of the inactive X chromosome (Xi) in female cells. By immunostaining of metaphase chromosomes from human lymphocytes with antibodies to the acetylated isoforms of histones H2A and H3, we now show that these histones too are underacetylated in both Xi and centric heterochromatin. Xi shows two prominent regions of residual H3 acetylation, one encompassing the pseudoautosomal region at the end of the short arm and one at about Xq22. Both these regions have been shown previously to be sites of residual H4 acetylation. H2A acetylation on Xi is higher overall than that of H3 or H4 and is particularly high around the pseudoautosomal region, but not at Xq22. The results suggest that the acetylated isoforms of H3 and H4 have at least some effects on chromosomal structure and function that are not shared by acetylated H2A.
Belyaev
N
N
Chromatin and Gene Expression Group, Anatomy Department, University of Birmingham Medical School, Edgbaston, UK.
Keohane
A M
AM
Turner
B M
BM
D000107:Acetylation; D000595:Amino Acid Sequence; D002874:Chromosome Mapping; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007621:Karyotyping; D008214:Lymphocytes / Q000166:cytology / Q000502:physiology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000276:immunology; D014960:X Chromosome
D006657:Histones; D010446:Peptide Fragments