Nucleic Acids Research, Vol 26, Issue 13 3111-3118, Copyright © 1998 by Oxford University Press
Z Karetsou, R Sandaltzopoulos, M Frangou-Lazaridis, CY Lai, O Tsolas, PB Becker and T Papamarcaki
Prothymosin alpha (ProTalpha) is an abundant acidic nuclear protein that
may be involved in cell proliferation. In our search for its cellular
partners, we have recently found that ProTalpha binds to linker histone H1.
We now provide further evidence for the physiological relevance of this
interaction by immunoisolation of a histone H1-ProTalpha complex from NIH
3T3 cell extracts. A detailed analysis of the interaction between the two
proteins suggests contacts between the acidic region of ProTalpha and
histone H1. In the context of a physiological chromatin reconstitution
reaction, the presence of ProTalpha does not affect incorporation of an
amount of histone H1 sufficient to increase the nucleosome repeat length by
20 bp, but prevents association of all further H1. Consistent with this
finding, a fraction of histone H1 is released when H1-containing chromatin
is challenged with ProTalpha. These results imply at least two different
interaction modes of H1 with chromatin, which can be distinguished by their
sensitivity to ProTalpha. The properties of ProTalpha suggest a role in
fine tuning the stoichiometry and/or mode of interaction of H1 with
chromatin.
ARTICLES
Prothymosin alpha modulates the interaction of histone H1 with chromatin
Laboratory of Biological Chemistry, University of Ioannina, Medical School, 451 10 Ioannina, Greece.
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