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

Khadake, JR and Markose, ER and Rao, MR (1994) Testis-specific histone (H1t) is not phosphorylated and has a weak interaction with chromatin. In: Indian Journal of Biochemistry & Biophysics, 31 (4). 335-338 .

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Soluble chromatin was prepared from rat testes after a brief micrococcal nuclease digestion. After adsorption onto hydroxylapatite at low ionic strength, the histone Hl subtypes were eluted with a shallow salt gradient of 0.3 M NaCl to 0.7 M NaCl. Histone Hlt was eluted at 0.4 MNaCl, while histones H1a and Hlc 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 Hlt, the major DNA binding domain of histone Hl, from that of the somatic consensus sequence may contribute to the weaker interaction of histone Hlt with the rat testis chromatin. Further, histone Hlt was not phosphorylated in vivo in contrast to histone Hla and Hlc, as is evident from the observation that histone Hlt lacks the SPKK motif recognized by the CDC-2kinase or the RR/KXS motif recognized by protein kinase A.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to National institute of science communication and information resources.
Department/Centre: Division of Biological Sciences > Biochemistry
Depositing User: Ms V Mangala
Date Deposited: 15 Apr 2011 05:11
Last Modified: 15 Apr 2011 05:11
URI: http://eprints.iisc.ac.in/id/eprint/36871

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