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Histone- and chromatin-binding activity of template activating factor-I
K Matsumoto1, K Nagata, M Okuwaki
1Laboratory of Cellular Biochemistry, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama, Japan. matsumok@postman.riken.go.jp
FEBS Letters
|December 22, 1999
Abstract:
Template activating factor-I (TAF-I) is a histone-binding chromatin remodeling factor. We recently found that TAF-I is capable of mediating decondensation of Xenopus sperm chromatin by releasing sperm-specific basic proteins. Here we present evidence that TAF-I preferentially binds to histone H3 among four core histones. Immunofluorescent staining revealed that TAF-I binds to the decondensed sperm chromatin, of which protein components predominantly consist of histones H3 and H4.