Testis-specific histone (H1t) is not phosphorylated and has a weak interaction with chromatin.

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dc.contributor.authorKhadake, J Ren_US
dc.contributor.authorMarkose, E Ren_US
dc.contributor.authorRao, M Ren_US
dc.date.accessioned1994-08-01en_US
dc.date.accessioned2009-05-27T09:41:52Z
dc.date.available1994-08-01en_US
dc.date.available2009-05-27T09:41:52Z
dc.date.issued1994-08-01en_US
dc.description.abstractSoluble chromatin was prepared from rat testes after a brief micrococcal nuclease digestion. After adsorption onto hydroxylapatite at low ionic strength, the histone H1 subtypes were eluted with a shallow salt gradient of 0.3 M NaCl to 0.7 M NaCl. Histone H1t was eluted at 0.4 M NaCl, while histones H1a and H1c were eluted at 0.43 M NaCl and 0.45 M respectively. The extreme divergence of the amino acid sequence of the C-terminal half of histone H1t, the major DNA binding domain of histone H1, from that of the somatic consensus sequence may contribute to the weaker interaction of histone H1t with the rat testis chromatin. Further, histone H1t was not phosphorylated in vivo in contrast to histone H1a and H1c, as is evident from the observation that histone H1t lacks the SPKK motif recognized by the CDC-2kinase or the RR/KXS motif recognized by protein kinase A.en_US
dc.description.affiliationDepartment of Biochemistry, Indian Institute of Science, Bangalore.en_US
dc.identifier.citationKhadake JR, Markose ER, Rao MR. Testis-specific histone (H1t) is not phosphorylated and has a weak interaction with chromatin. Indian Journal of Biochemistry & Biophysics. 1994 Aug; 31(4): 335-8en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/28290
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChromatin --metabolismen_US
dc.subject.meshHistones --metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOrgan Specificity --physiologyen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshTestisen_US
dc.titleTestis-specific histone (H1t) is not phosphorylated and has a weak interaction with chromatin.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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