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Histone‐ and chromatin‐binding activity of template activating factor‐I
Author(s) -
Matsumoto Ken,
Nagata Kyosuke,
Okuwaki Mitsuru,
Tsujimoto Masafumi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01632-4
Subject(s) - chromatin , histone , histone h1 , chromatin remodeling , microbiology and biotechnology , histone code , biology , chemistry , histone h2a , chromatin immunoprecipitation , histone h3 , biochemistry , nucleosome , dna , gene expression , promoter , gene
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.