DSpace Repository

Acetylation of Transition Protein 2 (TP2) by KAT3B (p300) Alters Its DNA Condensation Property and Interaction with Putative Histone Chaperone NPM3

Show simple item record

dc.contributor.author Pradeepa, Madapura M
dc.contributor.author Nikhil, Gupta
dc.contributor.author Kishore, Annavarapu Hari
dc.contributor.author Bharath, Giriyapura N
dc.contributor.author Kundu, Tapas K
dc.contributor.author Rao, M R S
dc.date.accessioned 2012-03-06T07:06:06Z
dc.date.available 2012-03-06T07:06:06Z
dc.date.issued 2009-10-23
dc.identifier 0021-9258 en_US
dc.identifier.citation Journal Of Biological Chemistry 284(43), 29956-29967 (2009) en_US
dc.identifier.uri https://libjncir.jncasr.ac.in/xmlui/10572/565
dc.description Restricted Access en_US
dc.description.abstract The hallmark of mammalian spermiogenesis is the dramatic chromatin remodeling process wherein the nucleosomal histones are replaced by the transition proteins TP1, TP2, and TP4. Subsequently these transition proteins are replaced by the protamines P1 and P2. Hyperacetylation of histone H4 is linked to their replacement by transition proteins. Here we report that TP2 is acetylated in vivo as detected by anti-acetylated lysine antibody and mass spectrometric analysis. Further, recombinant TP2 is acetylated in vitro by acetyltransferase KAT3B (p300) more efficiently than by KAT2B (PCAF). In vivo p300 was demonstrated to acetylate TP2. p300 acetylates TP2 in its C-terminal domain, which is highly basic in nature and possesses chromatin-condensing properties. Mass spectrometric analysis showed that p300 acetylates four lysine residues in the C-terminal domain of TP2. Acetylation of TP2 by p300 leads to significant reduction in its DNA condensation property as studied by circular dichroism and atomic force microscopy analysis. TP2 also interacts with a putative histone chaperone, NPM3, wherein expression is elevated in haploid spermatids. Interestingly, acetylation of TP2 impedes its interaction with NPM3. Thus, acetylation of TP2 adds a new dimension to its role in the dynamic reorganization of chromatin during mammalian spermiogenesis. en_US
dc.description.sponsorship Department of Biotechnology, Ministry of Science and Technology, New Delhi, India. Council of Scientific and Industrial Research, New Delhi, India. en_US
dc.description.uri http://dx.doi.org/10.1074/jbc.M109.052043 en_US
dc.language.iso en en_US
dc.publisher American Society for Biochemistry and Molecular Biology Inc en_US
dc.rights © 2009 The American Society for Biochemistry and Molecular Biology Inc en_US
dc.subject Mouse Spermatogenesis en_US
dc.subject Nucleic-Acids en_US
dc.subject Kinase-A en_US
dc.subject Transcription en_US
dc.subject Spermiogenesis en_US
dc.subject Identification en_US
dc.subject Involvement en_US
dc.subject Sperm en_US
dc.subject Mice en_US
dc.subject Hyperacetylation en_US
dc.title Acetylation of Transition Protein 2 (TP2) by KAT3B (p300) Alters Its DNA Condensation Property and Interaction with Putative Histone Chaperone NPM3 en_US
dc.type Article en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search DSpace


Advanced Search

Browse

My Account