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Mol Cell Biol, July 1998, p. 4315-4323, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA

Michal Goldberg,1 Huihua Lu,2 3 Nico Stuurman,4 Ruth Ashery-Padan,1 Aryeh M. Weiss,5 Jing Yu,2 3 Debika Bhattacharyya,2 Paul A. Fisher,6 Yosef Gruenbaum,1 and Mariana F. Wolfner2 *

Department of Genetics, The Life Sciences Institute, The Hebrew University of Jerusalem, Jerusalem 91904,1 and Department of Electronics, Jerusalem College of Technology, Jerusalem 91160,5 Israel; Section of Genetics and Development2 and Section of Biochemistry, Molecular and Cell Biology,3 Cornell University, Ithaca, New York 14853; M. E. Mueller-Institute for Microscopy, Biozentrum, University of Basel, Basel, Switzerland4; and Department of Pharmacological Sciences, Health Sciences Center, State University of New York at Stony Brook, Stony Brook, New York 117946

Received 19 November 1997/Returned for modification 16 January 1998/Accepted 22 April 1998

The nuclear envelope plays many roles, including organizing nuclear structure and regulating nuclear events. Molecular associations of nuclear envelope proteins may contribute to the implementation of these functions. Lamin, otefin, and YA are the three Drosophila nuclear envelope proteins known in early embryos. We used the yeast two-hybrid system to explore the interactions between pairs of these proteins. The ubiquitous major lamina protein, lamin Dm, interacts with both otefin, a peripheral protein of the inner nuclear membrane, and YA, an essential, developmentally regulated protein of the nuclear lamina. In agreement with this interaction, lamin and otefin can be coimmunoprecipitated from the vesicle fraction of Drosophila embryos and colocalize in nuclear envelopes of Drosophila larval salivary gland nuclei. The two-hybrid system was further used to map the domains of interaction among lamin, otefin, and YA. Lamin's rod domain interacts with the complete otefin protein, with otefin's hydrophilic NH2-terminal domain, and with two different fragments derived from this domain. Analogous probing of the interaction between lamin and YA showed that the lamin rod and tail plus part of its head domain are needed for interaction with full-length YA in the two-hybrid system. YA's COOH-terminal region is necessary and sufficient for interaction with lamin. Our results suggest that interactions with lamin might mediate or stabilize the localization of otefin and YA in the nuclear lamina. They also suggest that the need for both otefin and lamin in mediating association of vesicles with chromatin might reflect the function of a protein complex that includes these two proteins.

* Corresponding author. Mailing address: Section of Genetics and Development, Cornell University, Ithaca, NY 14853. Phone: (607) 254-4801. Fax: (607) 255-6249. E-mail: mfw5{at}cornell.edu.

Mol Cell Biol, July 1998, p. 4315-4323, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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