ArticleProceedings of the National Academy of Sciences of the United States of America1989
Identification and characterization of a nuclear localization sequence-binding protein in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 69 citations in OpenAlex.
- Conditionally controlling nuclear trafficking in yeast by chemical-induced protein dimerization.Nature protocols · 2010Article
- Characterization of a Drosophila phosphorylation-dependent nuclear-localization-signal-binding protein.The Biochemical journal · 1997Article
- Sequences within the VP6 molecule of bluetongue virus that determine cytoplasmic and nuclear targeting of the protein.Journal of virology · 1996Article
- Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I.The Journal of cell biology · 1996Article
- Nuclear localization signal binding proteins in higher plant nuclei.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Isolation and characterization of two Saccharomyces cerevisiae genes that encode proteins that bind to (TG1-3)n single strand telomeric DNA in vitro.Nucleic acids research · 1994Article
- Nucleocytoplasmic transport.The Biochemical journal · 1994Review
- The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals.The Plant cell · 1994Article
- Determination of the functional domains involved in nucleolar targeting of nucleolin.Molecular biology of the cell · 1993Article
- Multiple regions of NSR1 are sufficient for accumulation of a fusion protein within the nucleolus.The Journal of cell biology · 1993Article
- The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Specific binding of nuclear localization sequences to plant nuclei.The Plant cell · 1993Article
- Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae.Genetics · 1993Article
- NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex.Molecular biology of the cell · 1993Article
- Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins.The Journal of cell biology · 1992Article
- Enhancement of polyhedrin nuclear localization during baculovirus infection.Journal of virology · 1992Article
- A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1.The EMBO journal · 1992Article
- NIP1, a gene required for nuclear transport in yeast.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- NSR1 is required for pre-rRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits.Molecular and cellular biology · 1992Article
- A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast.Molecular biology of the cell · 1992Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear proteins contain specific regions that are required for entry into the nucleus. Using ligand blotting, we have shown that a 67-kDa yeast nuclear envelope protein (p67) recognizes synthetic peptides containing the yeast histone H2B or simian virus 40 large tumor antigen nuclear localization sequence. Both free peptide and peptide conjugated to human serum albumin are recognized. The interaction between p67 and the nuclear localization sequences is specific; neither a mutant peptide that is incompetent for nuclear transport in vivo nor HSA can interact with p67 on blots. Moreover, although the wild-type peptide competes for binding to p67, the mutant peptides do not. p67 appears to be located at the nuclear envelope and is not present in other subcellular fractions. The nuclear localization sequence-binding protein is not extracted from the nuclear envelope with nonionic detergents and only partially extracted with high-salt buffer or 8 M urea, suggestive of a tight association with the nuclear envelope. Together our results are consistent with a role for p67 in nuclear transport.
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