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© The Rockefeller University Press, 0021-9525/2002/8/475 $5.00
The Journal of Cell Biology, Volume 158, Number 3, August 5, 2002 475-485

Barrier-to-autointegration factor

Miriam Segura-Totten¹, Amy K. Kowalski¹, Robert Craigie² and Katherine L. Wilson¹

¹ Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205
² Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892

Address correspondence to Katherine L. Wilson, Dept. of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205. Tel.: (410) 955-1801. Fax: (410) 955-4129. E-mail: klwilson{at}jhmi.edu

Barrier-to-autointegration factor (BAF) is a DNA-bridging protein, highly conserved in metazoans. BAF binds directly to LEM (LAP2, emerin, MAN1) domain nuclear membrane proteins, including LAP2 and emerin. We used site-directed mutagenesis and biochemical analysis to map functionally important residues in human BAF, including those required for direct binding to DNA or emerin. We also tested wild-type BAF and 25 point mutants for their effects on nuclear assembly in Xenopus egg extracts, which contain 12 µM endogenous BAF dimers. Exogenous BAF caused two distinct effects: at low added concentrations, wild-type BAF enhanced chromatin decondensation and nuclear growth; at higher added concentrations, wild-type BAF completely blocked chromatin decondensation and nuclear growth. Mutants fell into four classes, including one that defines a novel functional surface on the BAF dimer. Our results suggest that BAF, unregulated, potently compresses chromatin structure, and that BAF interactions with both DNA and LEM proteins are critical for membrane recruitment and chromatin decondensation during nuclear assembly.

Key Words: HIV; retroviral preintegration complex; nucleus; emerin; nuclear envelope

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