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Originally published as MBC in Press, 10.1091/mbc.01-07-0336 on January 18, 2002
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Vol. 13, Issue 2, 558-569, February 2002

The Drosophila Nuclear Lamina Protein YA Binds to DNA and Histone H2B with Four Domains

Jing Yu,* and Mariana F. Wolfnerdagger

Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853-2703

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.

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

* Present address: Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138.

Molecular Biology of the Cell
Vol. 13, 558-569, February 2002
Copyright © 2002 by The American Society for Cell Biology


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