Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/596
Full metadata record
DC FieldValueLanguage
dc.contributor.authorUllas, Kolthur S-
dc.contributor.authorRao, M R S-
dc.date.accessioned2012-03-12T11:26:44Z-
dc.date.available2012-03-12T11:26:44Z-
dc.date.issued2003-12-26-
dc.identifier0021-9258en_US
dc.identifier.citationJournal Of Biological Chemistry 278(52), 52673-52680 (2003)en_US
dc.identifier.urihttp://hdl.handle.net/10572/596-
dc.descriptionRestricted Accessen_US
dc.description.abstractTransition protein 2 (TP2), which is expressed during stages 12-15 of mammalian spermiogenesis, has been shown to undergo phosphorylation immediately after its synthesis. We reported earlier that TP2 is phosphorylated in vitro at threonine 101 and serine 109 by the salt extract of sonication-resistant (elongating and elongated) spermatid nuclei and the protein kinase phosphorylating TP2 was identified to be protein kinase A (PKA). We now report that the cytosol from haploid spermatids but not from premeiotic germ cells is able to phosphorylate recombinant TP2 in vitro at threonine 101 and serine 109. The kinase present in the haploid spermatid cytosol that phosphorylates TP2 has been identified to be the sperm-specific isoform of protein kinase A (Cs-PKA). Reverse transcription-PCR analysis indicated that Cs-PKA was present in the haploid spermatids and absent from premeiotic germ cells. The rat Cs-PKA transcript was amplified and sequenced using the isoform-specific primers. The sequence of rat Cs-PKA at the N terminus differs from mouse and human by one amino acid. Western blot analysis using specific anti-Calpha1 antibodies revealed that Calpha1-PKA is absent in haploid spermatid cytosol. We have also established an in vitro nuclear transport assay for the haploid round spermatids. Using this assay, we have found that the cytoplasmic factors and ATP are absolutely essential for translocation of TP2 into the nucleus. Phosphorylation was found to positively modulate the NLS dependent import of TP2 into the nucleus.en_US
dc.description.urihttp://dx.doi.org/10.1074/jbc.M308365200en_US
dc.language.isoenen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology Incen_US
dc.rights© 2003 The American Society for Biochemistry and Molecular Biology Incen_US
dc.subjectSv40 T-Antigenen_US
dc.subjectCatalytic Subuniten_US
dc.subjectLocalization Signalen_US
dc.subjectRibosomal-Proteinsen_US
dc.subjectSomatic Histonesen_US
dc.subjectMammalian-Cellsen_US
dc.subjectImportin-Betaen_US
dc.subjectIi Siteen_US
dc.subjectC-Gammaen_US
dc.subjectChromatinen_US
dc.titlePhosphorylation of Rat Spermatidal Protein TP2 by Sperm-specific Protein Kinase A and Modulation of Its Transport into the Haploid Nucleusen_US
dc.typeArticleen_US
Appears in Collections:Research Papers (M.R.S. Rao)

Files in This Item:
File Description SizeFormat 
sl.no.100.2003 THE JOURNAL OF BIOLOGICAL CHEMISTRY 278(52) 52673–52680.pdf
  Restricted Access
593.05 kBAdobe PDFView/Open Request a copy


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.