Extensive and varied modifications in histone H2B of wild-type and histone deacetylase 1 mutant Neurospora crassa.
DNA methylation is deficient in a histone deacetylase 1 (HDA1) mutant (hda-1) strain of Neurospora crassa with inactivated histone deacetylase 1. Difference two-dimensional (2D) gels identified the primary histone deacetylase 1 target as histone H2B. Acetylation was identified by LC-MS/MS at five different lysines in wild-type H2B and at 11 lysines in hda-1 H2B, suggesting Neurospora H2B is a complex combination of different acetylated species. Individual 2D gel spots were shifted by single lysine acetylations. FTICR MS-observed methylation ladders identify an ensemble of 20-25 or more modified forms for each 2D gel spot. Twelve different lysines or arginines were methylated in H2B from the wild type or hda-1; only two were in the N-terminal tail. Arginines were modified by monomethylation, dimethylation, or deimination. H2B from wild-type and hda-1 ensembles may thus differ by acetylation at multiple sites, and by additional modifications. Combined with asymmetry-generated diversity in H2B structural states in nucleosome core particles, the extensive modifications identified here can create substantial histone-generated structural diversity in nucleosome core particles.
Anderson
D C
DC
Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA. dca0204@gmail.com
Green
George R
GR
Smith
Kristina
K
Selker
Eric U
EU
D000465:Algorithms; D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D056284:Histone Deacetylase 1 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D008745:Methylation; D008969:Molecular Sequence Data; D009492:Neurospora crassa / Q000201:enzymology*; D011499:Protein Processing, Post-Translational; D017550:Spectroscopy, Fourier Transform Infrared; D053719:Tandem Mass Spectrometry
D006657:Histones; D056284:Histone Deacetylase 1
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