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dc.contributor.authorChauhan, Sakshi
dc.contributor.authorMandal, Papita
dc.contributor.authorTomar, Raghuvir S.
dc.date.accessioned2017-01-02T09:08:23Z
dc.date.available2017-01-02T09:08:23Z
dc.date.issued2016-09-12
dc.identifier.citationChauhan S, Mandal P, Tomar RS (2016) Biochemical Analysis Reveals the Multifactorial Mechanism of Histone H3 Clipping by Chicken Liver Histone H3 Protease. Biochemistry 55: 5464–5482. Available: http://dx.doi.org/10.1021/acs.biochem.6b00625.
dc.identifier.issn0006-2960
dc.identifier.issn1520-4995
dc.identifier.doi10.1021/acs.biochem.6b00625
dc.identifier.urihttp://hdl.handle.net/10754/622277
dc.description.abstractProteolytic clipping of histone H3 has been identified in many organisms. Despite several studies, the mechanism of clipping, the substrate specificity, and the significance of this poorly understood epigenetic mechanism are not clear. We have previously reported histone H3 specific proteolytic clipping and a protein inhibitor in chicken liver. However, the sites of clipping are still not known very well. In this study, we attempt to identify clipping sites in histone H3 and to determine the mechanism of inhibition by stefin B protein, a cysteine protease inhibitor. By employing site-directed mutagenesis and in vitro biochemical assays, we have identified three distinct clipping sites in recombinant human histone H3 and its variants (H3.1, H3.3, and H3t). However, post-translationally modified histones isolated from chicken liver and Saccharomyces cerevisiae wild-type cells showed different clipping patterns. Clipping of histone H3 N-terminal tail at three sites occurs in a sequential manner. We have further observed that clipping sites are regulated by the structure of the N-terminal tail as well as the globular domain of histone H3. We also have identified the QVVAG region of stefin B protein to be very crucial for inhibition of the protease activity. Altogether, our comprehensive biochemical studies have revealed three distinct clipping sites in histone H3 and their regulation by the structure of histone H3, histone modifications marks, and stefin B.
dc.description.sponsorshipThis work was supported by Grant BT/PR3997/MED/97/33/2011 from the Department of Biotechnology, Government of India, to R.S.T. CSIR is acknowledged for providing fellowship support to S.C.
dc.publisherAmerican Chemical Society (ACS)
dc.relation.urlhttp://pubs.acs.org/doi/full/10.1021/acs.biochem.6b00625
dc.titleBiochemical Analysis Reveals the Multifactorial Mechanism of Histone H3 Clipping by Chicken Liver Histone H3 Protease
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalBiochemistry
dc.contributor.institutionLaboratory of Chromatin Biology, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India
kaust.personMandal, Papita
dc.date.published-online2016-09-12
dc.date.published-print2016-09-27


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