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MBC in Press, published online ahead of print January 18, 2002
Mol. Biol. Cell 10.1091/mbc.01-07-0336

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Submitted on July 5, 2001
Revised on October 22, 2001
Accepted on November 16, 2001

The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains

Jing Yu1 and Mariana F. Wolfner2*

1 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14850-2703(present address: Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138)
2 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14850-2703

* Corresponding author. E-mail address: mfw5{at}cornell.edu.

Dramatic changes occur in nuclear organization and function during the critical developmental transition from meiosis to mitosis. The Drosophila nuclear lamina protein YA binds to chromatin and is uniquely required for this transition. In this study, we dissected YA's binding to chromatin. We found that YA can bind to chromatin directly and specifically. It binds to DNA but not RNA, with a preference for double-stranded DNA (linear or supercoiled) over single-stranded DNA. It also binds to histone H2B. YA's binding to DNA and histone H2B is mediated by four domains distributed along the length of the YA molecule. A model for YA function at the end of Drosophila female meiosis is proposed.




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