Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine.
Open accessAbstract
The nuclear pore complex contains a family of proteins ranging in molecular mass from 35 to 220 kDa that are glycosylated with O-linked N-acetylglucosamine (GlcNAc) residues. We sought to determine the primary sequence of a nuclear pore protein modified by O-linked GlcNAc. The major (62 kDa) nuclear pore glycoprotein (np62) was purified from rat liver nuclear envelopes by immunoaffinity chromatography and preparative gel electrophoresis. After CNBr fragmentation, a glycopeptide was isolated and microsequenced. An oligonucleotide probe based on this sequence information was used to screen a lambda gt11 cDNA library constructed from poly(A) mRNA of the rat thyroid cell line FRTL-5. A clone (B5) was isolated and shown to hybridize to a single 2.5-kilobase species in poly(A) mRNA from rat liver and FRTL-5. This insert was sequenced and found to contain a 691-base-pair cDNA encoding a 155-amino acid open reading frame. This open reading frame contained a CNBr fragment identical to the original glycopeptide sequence and a second CNBr fragment corresponding to a nonglycosylated peptide that was also isolated from the purified pore glycoprotein. The B5 cDNA produced a beta-galactosidase fusion protein of the size predicted by the open reading frame. Analysis of the residues making up a presumptive glycosylation site suggests that the sequence is unlike any known sites for enzymatic N- or O-linked glycosylation. The partial sequence of the 62-kDa nuclear pore glycoprotein shows little similarity to other characterized proteins and elucidates structural features of a member of the family of nuclear pore glycoproteins.
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- Authors
- D'Onofrio, M., Starr, C. M., Park, M. K., Holt, G. D., Haltiwanger, R. S., Hart, G. W., & Hanover, J. A.
- Affiliations
- Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892.
- National Institutes of Health (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1988-12
- Volume
- 85
- Issue
- 24
- Pages
- 9595-9599
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC282808
- OpenAlex
- W2067098156
- Cited by
- 63
- References
- 26
- Citations by year
- 2021: 1 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 1 · 2013: 2
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- nuclear pore complex, O-GlcNAc, glycosylation, cDNA cloning, glycosylation sites, nuclear envelope, rat liver, beta-galactosidase fusion protein
- MeSH terms
- Acetylglucosamine, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Glucosamine, Liver, Membrane Glycoproteins, Membrane Proteins, Molecular Sequence Data, Molecular Weight, Nuclear Envelope, Peptide Mapping, Nuclear Pore Complex Proteins, Rats
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