The class I histone deacetylases of the platyhelminth parasite Schistosoma mansoni.

Abstract:

:Histone deacetylases (HDAC) form a conserved enzyme family that control gene expression via the removal of acetyl residues from histones and other proteins and are under increasing investigation as therapeutic targets, notably in cancer and parasitic diseases. To investigate the conservation of these enzymes in the platyhelminth parasite Schistosoma mansoni, we cloned and characterized three class I HDACs, orthologues of mammalian HDAC1, 3 and 8, and confirmed their identities by phylogenetic analysis. The identification of an HDAC8 orthologue showed that it is not vertebrate-specific as previously thought and insertions in its catalytic domain suggest specific enzymatic properties. SmHDAC1, 3, and 8 mRNAs are expressed at all schistosome life-cycle stages. SmHDAC1 repressed transcriptional activity in a mammalian cell line and this activity was dependent on its catalytic activity since transcription was partially restored by treatment with trichostatin A and a catalytic site mutant failed to repress transcription.

authors

Oger F,Dubois F,Caby S,Noël C,Cornette J,Bertin B,Capron M,Pierce RJ

doi

10.1016/j.bbrc.2008.10.090

subject

Has Abstract

pub_date

2008-12-26 00:00:00

pages

1079-84

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02085-8

journal_volume

377

pub_type

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