Mass spectrometric analysis of histone posttranslational modifications.
The uses of tandem and Fourier transform mass spectrometric methodologies for assignment of the posttranslational sites and occupancies of histones and their isoforms is described employing several illustrative examples. A comparison of information that can be obtained from intact protein sequencing and proteolytic digestion is presented.
Burlingame
A L
AL
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143-0446, USA. alb@itsa.ucsf.edu
Zhang
Xin
X
Chalkley
Robert J
RJ
D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D005583:Fourier Analysis; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007477:Ions / Q000737:chemistry; D008239:Lysine / Q000378:metabolism; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods; D008745:Methylation; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000295:instrumentation / Q000379:methods; D014357:Trypsin / Q000378:metabolism
D006657:Histones; D007477:Ions; D010446:Peptide Fragments; D014357:Trypsin; D008239:Lysine