Testis-specific histone (H1t) is not phosphorylated and has a weak interaction with chromatin.
No Thumbnail Available
Date
1994-08-01
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Soluble 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.
Description
Keywords
Citation
Khadake 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): 335-8