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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

A PHD finger of NURF couples histone H3 c 4 trimethylation with chromatin remodelling

Article Abstract:

A plant homeodomain (PHD) finger of nucleosome remodeling factor (NURF), an ATP-dependent chromatin-remodeling complex, is shown to mediate a direct preferential association with trimethylation of histone H3 lysine4 (H3K4me3) tails. Results suggest that protein WDR5 and NURF function in a common biological pathway in vivo, and that NURF-mediated ATP-dependent chromatin remodeling is directly coupled to H3K4 trimethylation to maintain Hox gene expression patterns during development.

Author: Allis, C. David, Wu, Carl, Chait, Brian T., Milne, Thomas A., Wysocka, Joanna, Swigut, Tomek, Tackett, Alan J., Badenhorst, Paul, Hua Xiao, So Yeon Kwon, Landry, Joe, Kauer, Monika
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
Maryland, Gene expression, Methylation, Lysine, Properties

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Structural similarity between TAF and the heterotetrameric core of the histone octamer

Article Abstract:

Two TFIID TATA box-binding protein-associated factors (TAF) are presented in a 2.0A resolution structure. The amin-terminal segment of dTAF42 and dTAF62 from Drosophila use the canonical histone fold. It is concluded that the 2.0A resolution structure of the dTAF42/dTAF62 complex gives the first structural knowledge of RNA polymerase II TAFs. The research work represents the starting point for crystallographic, biochemical and genetic studies of TFIID assembly.

Author: Burley, Stephen K., Nakatani, Yoshihiro, Chait, Brian T., Roeder, Robert G., Hoffmann, Alexander, Xiaoling Xie, Kokubo, Tetsuro, Cohen, Steven L., Mirza, Urooj A.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Genetic research

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Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment

Article Abstract:

Heat shock factor (HSF), which binds DNA, appears to be activated less by changes in temperature than by the reaction to those changes of the cell containing the protein. Human HSF expressed in Drosophila cells showed DNA binding and trimerization at about 10 degrees C less than necessary in human cells, whereas Drosophila HSF showed no change in human cells. Human HSF also acts at a lower temperature when expressed in tobacco protoplasts.

Author: Wu, Carl, Clos, Joachim, Rabindran, Sridhar, Wisniewski, Jan
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Research, Heat shock proteins

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Subjects list: Analysis, Physiological aspects, Genetic aspects, Drosophila
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