TY - JOUR
T1 - Revealing histone variant induced changes via quantitative proteomics
AU - Arnaudo, Anna M.
AU - Molden, Rosalynn C.
AU - Garcia, Benjamin A.
N1 - Funding Information:
The authors declare no conflict of interest. B.A.G is supported by the American Society for Mass Spectrometry Research award sponsored by the Waters Corp., an NJCCR SEED grant, an NSF Faculty CAREER award, an NSF grant (CBET-0941143), an Agilent Thought Leader award, and an NIH Innovator award (DP2OD007447) from the Office Of The Director, NIH.
PY - 2011/8
Y1 - 2011/8
N2 - Histone variants are isoforms of linker and core histone proteins that differ in their amino acid sequences. These variants have distinct genomic locations and posttranslational modifications, thus increasing the complexity of the chromatin architecture. Biological studies of histone variants indicate that they play a role in many processes including transcription, DNA damage response, and the cell cycle. The small differences in amino acid sequence and the diverse posttranslational modification states that exist between histone variants make traditional analysis using immunoassay methods challenging. In recent years, a number of mass spectrometric techniques have been developed to identify and quantify histones at the whole protein or peptide levels. In this review, we discuss the biology of histone variants and methods to characterize them using mass spectrometry-based proteomics.
AB - Histone variants are isoforms of linker and core histone proteins that differ in their amino acid sequences. These variants have distinct genomic locations and posttranslational modifications, thus increasing the complexity of the chromatin architecture. Biological studies of histone variants indicate that they play a role in many processes including transcription, DNA damage response, and the cell cycle. The small differences in amino acid sequence and the diverse posttranslational modification states that exist between histone variants make traditional analysis using immunoassay methods challenging. In recent years, a number of mass spectrometric techniques have been developed to identify and quantify histones at the whole protein or peptide levels. In this review, we discuss the biology of histone variants and methods to characterize them using mass spectrometry-based proteomics.
UR - http://www.scopus.com/inward/record.url?scp=79960803077&partnerID=8YFLogxK
U2 - 10.3109/10409238.2011.577052
DO - 10.3109/10409238.2011.577052
M3 - Review article
C2 - 21526979
AN - SCOPUS:79960803077
SN - 1040-9238
VL - 46
SP - 284
EP - 294
JO - Critical Reviews in Biochemistry and Molecular Biology
JF - Critical Reviews in Biochemistry and Molecular Biology
IS - 4
ER -