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Molecular and Cellular Biology, October 1999, p. 6940-6952, Vol. 19, No. 10
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Sperm Chromatin Decondensation by Template Activating Factor I through Direct Interaction with Basic Proteins

Ken Matsumoto,1,* Kyosuke Nagata,2 Mary Miyaji-Yamaguchi,2 Akihiko Kikuchi,3 and Masafumi Tsujimoto1

Laboratory of Cellular Biochemistry, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-0198,1 Laboratory of Molecular Medical Engineering, Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501,2 and Research Institute for Disease Mechanism and Control, School of Medicine, Nagoya University, Nagoya 466-8550,3 Japan

Received 3 March 1999/Returned for modification 2 June 1999/Accepted 25 July 1999

Template activating factor I (TAF-I) was originally identified as a host factor required for DNA replication and transcription of adenovirus genome complexed with viral basic proteins. Purified TAF-I was shown to bind to core histones and stimulate transcription from nucleosomal templates. Human TAF-I consists of two acidic proteins, TAF-Ialpha and TAF-Ibeta , which differ from each other only in their amino-terminal regions. Here, we report that TAF-I decondenses demembraned Xenopus sperm chromatin. Human TAF-Ibeta has a chromatin decondensation activity comparable to that of NAP-I, another histone binding protein, whereas TAF-Ialpha has only a weak activity. Analysis of molecular mechanisms underlying the chromatin decondensation by TAF-I revealed that TAF-I interacts directly with sperm basic proteins. Deletion of the TAF-I carboxyl-terminal acidic region abolishes the decondensation activity. Interestingly, the acidic region itself is not sufficient for decondensation, since an amino acid substitution mutant in the dimerization domain of TAF-I which has the intact acidic region does not support chromatin decondensation. We detected the beta  form of TAF-I in Xenopus oocytes and eggs by immunoblotting, and the cloning of its cDNA led us to conclude that Xenopus TAF-Ibeta also decondenses sperm chromatin. These results suggest that TAF-I plays a role in remodeling higher-order chromatin structure as well as nucleosomal structure through direct interaction with chromatin basic proteins.

* Corresponding author. Mailing address: Laboratory of Cellular Biochemistry, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Phone: 81 48 462 1111. Fax: 81 48 462 4670. E-mail: matsumok{at}postman.riken.go.jp.

Molecular and Cellular Biology, October 1999, p. 6940-6952, Vol. 19, No. 10
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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