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dc.contributor.authorPradeepa, Madapura M-
dc.contributor.authorNikhil, Gupta-
dc.contributor.authorKishore, Annavarapu Hari-
dc.contributor.authorBharath, Giriyapura N-
dc.contributor.authorKundu, Tapas K-
dc.contributor.authorRao, M R S-
dc.date.accessioned2012-02-14T06:53:35Z-
dc.date.available2012-02-14T06:53:35Z-
dc.date.issued2009-10-23-
dc.identifier0021-9258en_US
dc.identifier.citationJournal Of Biological Chemistry 284(43), 29956-29967 (2009)en_US
dc.identifier.urihttp://hdl.handle.net/10572/403-
dc.descriptionRestricted Accessen_US
dc.description.abstractThe 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.sponsorshipDepartment of Biotechnology, Ministry of Science and Technology, New Delhi, India. Council of Scientific and Industrial Research, New Delhi, India.en_US
dc.description.urihttp://dx.doi.org/10.1074/jbc.M109.052043en_US
dc.language.isoenen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology Incen_US
dc.rights© 2009 The American Society for Biochemistry and Molecular Biology Incen_US
dc.subjectMouse Spermatogenesisen_US
dc.subjectNucleic-Acidsen_US
dc.subjectKinase-Aen_US
dc.subjectTranscriptionen_US
dc.subjectSpermiogenesisen_US
dc.subjectIdentificationen_US
dc.subjectInvolvementen_US
dc.subjectSpermen_US
dc.subjectMiceen_US
dc.subjectHyperacetylationen_US
dc.titleAcetylation of Transition Protein 2 (TP2) by KAT3B (p300) Alters Its DNA Condensation Property and Interaction with Putative Histone Chaperone NPM3en_US
dc.typeArticleen_US
Appears in Collections:Research Papers (Tapas K. Kundu)

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