Zebrafish HSF4: a novel protein that shares features of both HSF1 and HSF4 of mammals.

作者: Cynthia L. Swan , Tyler G. Evans , Nicole Sylvain , Patrick H. Krone

DOI: 10.1007/S12192-012-0337-3

关键词:

摘要: Heat-shock proteins (hsps) have important roles in the development of eye lens. We previously demonstrated that knockdown hsp70 gene expression using morpholino antisense technology resulted an altered lens phenotype zebrafish embryos. A less severe was seen with heat-shock factor 1 (HSF1), suggesting that, while it likely plays a role regulation during formation, other regulatory factors are also involved. 4 mammalian development, and expressed sequence tag encoding HSF4 has been identified. The deduced amino acid shares structural similarities including lack HR-C domain. However, domain is absent due to C-terminal truncation within (zHSF4) relative protein. Surprisingly, composition zHSF4 DNA binding greater degree identity HSF1 than does proteins. Consistent this, affinity vitro synthesized for discontinuous response element sequences more limited, similar what observed Hsf4 mRNA adult tissue but only developing embryonic at 60 h post-fertilization or later. This, together observable following morpholino-based hsf4, suggests unlikely play regulating early development.

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