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Journal of Biochemistry Advance Access originally published online on September 29, 2006
Journal of Biochemistry 2006 140(5):627-637; doi:10.1093/jb/mvj197
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© 2006 The Japanese Biochemical Society.

ARTICLE

Prothymosin {alpha} Interacts with Free Core Histones in the Nucleus of Dividing Cells

Guillermo Covelo, Concepción S. Sarandeses, Cristina Díaz-Jullien and Manuel Freire*

Departamento de Bioquímica y Biología Molecular, Facultad de Biología, Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain

* To whom correspondence should be addressed. Tel: +34-981-563100 (Ext. 13316), Fax: +34-981-596904, E-mail: bnfreire@usc.es

The acidic protein prothymosin {alpha} (ProT{alpha}), with a broad presence in mammalian cells, has been widely considered to have a role in cell division, through an unrevealed mechanism in which histones may be involved in view of their ability to interact with ProT{alpha} in vitro. Results of co-immunoprecipitation experiments presented here demonstrate that ProT{alpha} interacts in vivo with core histones in proliferating B-lymphocytes (NC-37 cells). This interaction occurs with histones H3, H2A, H2B and H4 located free in the nucleoplasm, whereas no interaction was detected with histone H1, mono-nucleosome particles or chromatin. Moreover, the core histones form part of a nuclear multiprotein complex of about 700 kDa separated by ProT{alpha}-Sepharose affinity, with components including H3 and H4 acetyltranferases, H3 methyltransferases, hnRNP isotypes A3, A2/B1 and R, ATP-dependent and independent DNA helicases II, ß-actin and vimentin, all co-purifying by gel filtration. This indicates that the interaction of ProT{alpha} with core histones in the nucleus may be related to the structural modification of histones H3 and H4, and hence to chromatin activity, raising the possibility that the other proteins in the nuclear complex may play a role in this process.


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