Two membrane proteins were identified through their genetic interaction wit
h the nucleoporin Nup84p and shown to participate in nuclear envelope morph
ogenesis in yeast. One component is a known sporulation factor Spo7p, and t
he other, Nem1p, a novel protein whose C-terminal domain is conserved durin
g eukaryotic evolution. Spo7p and Nem1p localize to the nuclear/ER membrane
and behave biochemically as integral membrane proteins, Nem1p binds to Spo
7p via its conserved C-terminal domain. Although cells without Spo7p or Nem
1p are viable, they exhibit a drastically altered nuclear morphology with l
ong, pore-containing double nuclear membrane extensions. These protrusions
emanate from a core nucleus which contains the DNA, and penetrate deeply in
to the cytoplasm, Interestingly, not only Spo7(-) and Nem1(-), but also sev
eral nucleoporin mutants are defective in sporulation, Thus, Spo7p and Nem1
p, which exhibit a strong genetic link to nucleoporins of the Nup84p comple
x, fulfil an essential role in formation of a spherical nucleus and meiotic
division.