Distinct regions specify the targeting of otefin to the nucleoplasmic side of the nuclear envelope

Ruth Ashery-Padan, Aryeh M. Weiss, Naomi Femstein, Yosef Gruenbaum*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

Otefin is a 45-kDa nuclear envelope protein with no apparent homology to other known proteins. It includes a large hydrophilic domain, a single carboxyl-terminal hydrophobic sequence of 17 amino acids, and a high content of serine and threonine residues. Cytological labeling located otefin on the nucleoplasmic side of the nuclear envelope. Chemical extraction of nuclei from Drosophila embryos revealed that otefin is a peripheral protein whose association with the nuclear envelope is stronger than that of lamin. Deletion mutants of otefin were expressed in order to identify regions that direct otefin to the nuclear envelope. These experiments revealed that the hydrophobic sequence at the carboxyl terminus is essential for correct targeting to the nuclear envelope, whereas additional regions in the hydrophilic domain of otefin are required for its efficient targeting and stabilization in the nuclear envelope.

Original languageEnglish
Pages (from-to)2493-2499
Number of pages7
JournalJournal of Biological Chemistry
Volume272
Issue number4
DOIs
StatePublished - 1997

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