Title
Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
6-1-2005
Document Type
Article
Subjects
Acetylation; Amino Acid Sequence; Binding Sites; Cell Cycle Proteins; Histone Acetyltransferases; Lysine; Molecular Sequence Data; Peptides; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transcription Factors; p300-CBP Transcription Factors
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Abstract
Matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry (MS/MS) were used to determine the multiple acetylation sites in the histone acetyltransferase (HAT): p300-HAT. Partial cleavage of the peptides containing acetylated lysine residues by trypsin provided a set of nested sequences that enabled us to determine that multiple acetylation occurs on the same molecule. At the same time, cleavages resulting in a terminal unacetylated lysine suggested that not all of these sites are fully modified. Using MS and MS/MS, we were able to characterize both the unmodified and acetylated tryptic peptides covering more than 82% of the protein.
Keywords
Acetylation, Amino acid sequencing, Matrix-assisted laser desorption/ionization-time of flight, Mass spectrometry
DOI of Published Version
10.1002/pmic.200401167
Source
Proteomics. 2005 Jun;5(9):2288-96. Link to article on publisher's site
Journal/Book/Conference Title
Proteomics
Related Resources
Repository Citation
Wang, Dongxia; Thompson, Paul R.; Cole, Philip A.; and Cotter, Robert J., "Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer" (2005). Thompson Lab Publications. 82.
https://escholarship.umassmed.edu/thompson/82
Comments
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.