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PMID: 2738089 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.

The Journal of cell biology ·Vol. 108 ·No. 6 ·1989-06-00 ·Pages 2083-92

Wozniak RW, Bartnik E, Blobel G

Abstract

The complete primary structure of an integral membrane glycoprotein of the nuclear pore was deduced from the cDNA sequence. The cDNA encodes a polypeptide of 204,205 D containing a 25-residue-long signal sequence, two hydrophobic segments that could function as transmembrane segments, and 13 potential N-linked oligosaccharide addition sites. Endoglycosidase H reduces the molecular mass by approximately 9 kD suggesting that not all of these 13 sites are used. We discuss possible models for the topology of this protein in the pore membrane as well as a possible role in the formation of pores and pore complexes.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cloning, Molecular DNA/genetics Hexosaminidases/metabolism Membrane Glycoproteins/genetics,ultrastructure Molecular Sequence Data Molecular Weight Nuclear Envelope/analysis,ultrastructure Rats Solubility
Chemicals
Membrane Glycoproteins DNA Hexosaminidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wozniak R W
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021.
Bartnik E
Blobel G
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.108.6.2083
Published
1989-06-00
Pages
2083-92
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2115607
Subset
IM
Databases
GENBANK
Y00826
External Links
PubMed source DOI: 10.1083/jcb.108.6.2083 PMC Full Text View journal details
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