Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/2362
Title: Mapping Post-translational Modifications of Mammalian Testicular Specific Histone Variant TH2B in Tetraploid and Haploid Germ Cells and Their Implications on the Dynamics of Nucleosome Structure
Authors: Pentakota, Satya Krishna
Sandhya, Sankaran
Sikarwar, Arun P.
Chandra, Nagasuma
Rao, M. R. S.
Keywords: Biochemical Research Methods
Mass Spectromety
Post-Translational Modifications
Nucleosome Models
Histone-Histone And Histone DNA Interactions
Mass-Spectrometry
Core Particle
Chromatin Modifications
Angstrom Resolution
Crystal-Structure
High-Throughput
N-Terminus
Protein
H2B
Spermatogenesis
Issue Date: 2014
Publisher: American Chemical Society
Citation: Pentakota, SK; Sandhya, S; Sikarwar, AP; Chandra, N; Rao, MRS, Mapping Post-translational Modifications of Mammalian Testicular Specific Histone Variant TH2B in Tetraploid and Haploid Germ Cells and Their Implications on the Dynamics of Nucleosome Structure. Journal of Proteome Research 2014, 13 (12) 5603-5617, http://dx.doi.org/10.1021/pr500597a
Journal of Proteome Research
13
12
Abstract: Histones regulate a variety of chromatin templated events by their post-translational modifications (PTMs). Although there are extensive reports on the PTMs of canonical histones, the information on the histone variants remains very scanty. Here, we report the identification of different PTMs, such as acetylation, methylation, and phosphorylation of a major mammalian histone variant TH2B. Our mass spectrometric analysis has led to the identification of both conserved and unique modifications across tetraploid spermatocytes and haploid spermatids. We have also computationally derived the 3-dimensional model of a TH2B containing nucleosome in order to study the spatial orientation of the PTMs identified and their effect on nucleosome stability and DNA binding potential. From our nucleosome model, it is evident that substititution of specific amino acid residues in TH2B results in both differential histone-DNA and histone-histone contacts. Furthermore, we have also observed that acetylation on the N-terminal tail of TH2B weakens the interactions with the DNA. These results provide direct evidence that, similar to somatic H2B, the testis specific histone TH2B also undergoes multiple PTMs, suggesting the possibility of chromatin regulation by such covalent modifications in mammalian male germ cells.
Description: Restricted Access
URI: http://hdl.handle.net/10572/2362
ISSN: 1535-3893
Appears in Collections:Research Papers (M.R.S. Rao)

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