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J. Biol. Chem., Vol. 265, Issue 14, 7808-7813, 05, 1990
R Padan, S Nainudel-Epszteyn, R Goitein, A Fainsod and Y Gruenbaum
We have recently identified and characterized a 53-kDa inner nuclear
membrane-associated protein in Drosophila and termed it otefin. Here we
report the isolation and characterization of cDNA and genomic clones of the
otefin gene. Based on sequence analysis, we deduced that the primary
translation product has a calculated mass of 45 kDa, contains many serine
and threonine residues, and is mostly hydrophilic. However, in the carboxyl
terminus, there is a hydrophobic region which may serve as a membrane
anchoring domain. RNA blot analysis indicated that the otefin gene codes
for a single poly(A+) transcript of 1.6 kilobases and that relatively large
amounts of this transcript are present during developmental stages in which
many nuclear divisions occur. Polyclonal antibodies raised against the cDNA
translation product react with a 58- kDa mammalian nuclear envelope
protein, demonstrating evolutionary conservation.
Isolation and characterization of the Drosophila nuclear envelope otefin cDNA
Department of Genetics, Hebrew University of Jerusalem, Israel.
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