Abstract:
:The HIRIP3 protein had been identified from its interaction with the HIRA histone chaperone. Experiments using anti-peptide antisera indicated that this 556-aa protein is nuclear throughout the cell cycle and excluded from condensed chromatin during mitosis. Based on its electrophoretic migration and sensitivity to phosphatase treatment, endogenous HIRIP3 was found to be heavily phosphorylated. HIRIP3 can be phosphorylated in vitro by a recombinant form of the serine-threonine kinase CK2. Moreover, HIRIP3 protein was found to co-purify with a CK2 activity. Together, these data prompt us to propose HIRIP3 as a new member of the growing list of CK2 substrates with a possible role in chromatin metabolism.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Assrir N,Filhol O,Galisson F,Lipinski Mdoi
10.1515/BC.2007.045subject
Has Abstractpub_date
2007-04-01 00:00:00pages
391-8issue
4eissn
1431-6730issn
1437-4315journal_volume
388pub_type
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