Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine.

M D'Onofrio1, C M Starr, M K Park

  • 1Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892.

Proceedings of the National Academy of Sciences of the United States of America
|December 1, 1988
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

An exploratory (1) H-nuclear magnetic resonance metabolomics study reveals altered urine spectral profiles in infants with atopic dermatitis.

The British journal of dermatology·2011
Same author

Observation of the Ξ(b)(0) baryon.

Physical review letters·2011
Same author

Measurement of the cross section for prompt isolated diphoton production in pp collisions at square root(s) = 1.96  TeV.

Physical review letters·2011
Same author

The EFSUMB Guidelines and Recommendations on the Clinical Practice of Contrast Enhanced Ultrasound (CEUS): update 2011 on non-hepatic applications.

Ultraschall in der Medizin (Stuttgart, Germany : 1980)·2011
Same author

Measurement of the W+ W- cross section in sqrt(s) = 7  TeV pp collisions with ATLAS.

Physical review letters·2011
Same author

First search for multijet resonances in sqrt(s) = 1.96  TeV pp collisions.

Physical review letters·2011

Researchers identified the primary sequence of a major nuclear pore glycoprotein (np62) using O-linked N-acetylglucosamine (GlcNAc) modification. This finding advances understanding of nuclear pore complex protein structure and glycosylation.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Nuclear pore complex (NPC) proteins are crucial for nucleocytoplasmic transport.
  • A subset of NPC proteins are modified with O-linked N-acetylglucosamine (GlcNAc).
  • The specific sequences and functions of these glycosylated NPC proteins remain largely uncharacterized.

Purpose of the Study:

  • To determine the primary amino acid sequence of a major glycosylated nuclear pore protein.
  • To elucidate structural features of O-linked GlcNAc modified nuclear pore glycoproteins.
  • To investigate potential novel glycosylation sites within nuclear pore proteins.

Main Methods:

  • Purification of the 62 kDa nuclear pore glycoprotein (np62) from rat liver nuclear envelopes.
  • Immunoaffinity chromatography and preparative gel electrophoresis for protein isolation.

Related Experiment Videos

  • CNBr fragmentation, glycopeptide microsequencing, and cDNA library screening (lambda gt11) for sequence determination.

    • Main Results:

    • A 691-base-pair cDNA encoding a 155-amino acid open reading frame for np62 was isolated and sequenced.
    • The deduced sequence contained fragments matching the microsequenced glycopeptide and a nonglycosylated peptide.
    • Analysis revealed a presumptive glycosylation site dissimilar to known enzymatic glycosylation sites.
    • The np62 sequence showed limited similarity to other known proteins.

    Conclusions:

    • The primary sequence of the major 62 kDa nuclear pore glycoprotein (np62) has been elucidated.
    • This study provides insights into the structural characteristics of O-linked GlcNAc modified nuclear pore proteins.
    • The identified glycosylation site suggests a potentially novel mechanism of O-GlcNAc modification in the nuclear pore complex.