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.
Department of Genetics,
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.
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