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Vol. 11, Issue 9, 3089-3099, September 2000
*Department of Cell Biology and Anatomy, The Johns Hopkins
University School of Medicine, Baltimore, Maryland 21205;
Emerin, MAN1, and LAP2 are integral membrane proteins of the
vertebrate nuclear envelope. They share a 43-residue N-terminal motif
termed the LEM domain. We found three putative LEM domain genes in
Caenorhabditis elegans, designated emr-1,
lem-2, and lem-3. We analyzed
emr-l, which encodes Ce-emerin, and
lem-2, which encodes Ce-MAN1. Ce-emerin and Ce-MAN1
migrate on SDS-PAGE as 17- and 52-kDa proteins, respectively. Based on
their biochemical extraction properties and immunolocalization, both
Ce-emerin and Ce-MAN1 are integral membrane proteins localized at the
nuclear envelope. We used antibodies against Ce-MAN1, Ce-emerin,
nucleoporins, and Ce-lamin to determine the timing of nuclear envelope
breakdown during mitosis in C. elegans. The C.
elegans nuclear envelope disassembles very late compared with
vertebrates and Drosophila. The nuclear membranes
remained intact everywhere except near spindle poles during metaphase
and early anaphase, fully disassembling only during mid-late anaphase.
Disassembly of pore complexes, and to a lesser extent the lamina,
depended on embryo age: pore complexes were absent during metaphase in
>30-cell embryos but existed until anaphase in 2- to 24-cell embryos.
Intranuclear mRNA splicing factors disassembled after prophase. The
timing of nuclear disassembly in C. elegans is novel and
may reflect its evolutionary position between unicellular and more
complex eukaryotes.
Department of Genetics, The Institute of Life Sciences,
The Hebrew University of Jerusalem, Jerusalem 91904, Israel; and
§Department of Embryology, Carnegie Institute of
Washington, Baltimore, Maryland 21210
These authors contributed equally to this work.
Corresponding author. E-mail address:
klwilson{at}jhmi.edu.
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