TY - JOUR
T1 - Distinct regions specify the targeting of otefin to the nucleoplasmic side of the nuclear envelope
AU - Ashery-Padan, Ruth
AU - Weiss, Aryeh M.
AU - Femstein, Naomi
AU - Gruenbaum, Yosef
PY - 1997
Y1 - 1997
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0031029561&partnerID=8YFLogxK
U2 - 10.1074/jbc.272.4.2493
DO - 10.1074/jbc.272.4.2493
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C2 - 8999964
AN - SCOPUS:0031029561
SN - 0021-9258
VL - 272
SP - 2493
EP - 2499
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 4
ER -