Histone- and chromatin-binding activity of template activating factor-I.
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.
Matsumoto
K
K
Laboratory of Cellular Biochemistry, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama, Japan. matsumok@postman.riken.go.jp
Nagata
K
K
Okuwaki
M
M
Tsujimoto
M
M
D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone; D005982:Glutathione Transferase; D006657:Histones / Q000378:metabolism*; D008297:Male; D009687:Nuclear Proteins / Q000378:metabolism / Q000494:pharmacology*; D013094:Spermatozoa / Q000378:metabolism*; D013698:Templates, Genetic; D014157:Transcription Factors; D014981:Xenopus
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D009687:Nuclear Proteins; D014157:Transcription Factors; C026588:sperm basic nuclear proteins; D005982:Glutathione Transferase