Title : Ion Mobility-Mass Spectrometry Reveals Evidence of Specific Complex Formation between Human Histone Deacetylase 8 and Poly-r(C)-binding Protein 1.

Pub. Date : 2017 Sep

PMID : 28983190






3 Functional Relationships(s)
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Protein Name
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1 Recent evidence, however, has linked this protein to iron incorporation, loaded through transient interactions with the poly r(C)-binding protein 1, a metallo-chaperone and storage protein. Iron poly(rC) binding protein 1 Homo sapiens
2 Furthermore, our data strongly support that complexes between histone deacetylase 8 and poly r(C)-binding protein 1 are specific, and that they are equally strong when both zinc and iron-loaded proteins are involved, or perhaps mildly promoted in the latter case, suggesting an in vivo role for the non-canonical, iron-incorporated histone deacetylase. Iron poly(rC) binding protein 1 Homo sapiens
3 Furthermore, our data strongly support that complexes between histone deacetylase 8 and poly r(C)-binding protein 1 are specific, and that they are equally strong when both zinc and iron-loaded proteins are involved, or perhaps mildly promoted in the latter case, suggesting an in vivo role for the non-canonical, iron-incorporated histone deacetylase. Iron poly(rC) binding protein 1 Homo sapiens