The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins
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Jutta Mayr
Abstract
Wild-type proteasomes of human erythrocytes and the archaeon Thermoplasma acidophilum compete with each other for transport into nuclei of digitonin-permeabilized HeLa cells in the presence of an energy-regenerating system and rabbit reticulocyte lysate. ‘NLS’-mutated Thermoplasma proteasomes were also able to compete with human proteasomes in the same assay, although with lower efficiency. Furthermore, in contrast to the other archaeal and bacterial cell lysates tested, the Thermoplasma cytosol efficiently supported nuclear import of human and Thermoplasma proteasomes. However, the same lysate could barely direct the nuclear transport of BSA-NLSSV40 peptide conjugates or the classical NLS-bearing protein, nucleoplasmin. Finally, additional importin α/β significantly decreased the import efficiency of both human and Thermoplasma proteasomes. Taken together, these results suggest that nuclear import of proteasomes may use a novel pathway that is different from that of classical NLS-bearing proteins.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Editors Note
- Walter Neupert: Spellbound by Mitochondria
- Posttranslational Protein Translocation Across the Membrane of the Endoplasmic Reticulum
- Import of Carrier Proteins into Mitochondria
- The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
- Mitochondrial Iron Metabolism in the Yeast Saccharomyces cerevisiae
- A Scj1p Homolog and Folding Catalysts Present in Dog Pancreas Microsomes
- The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins
- Role of p52 (NF-kappaB2) in LPS Tolerance in a Human B Cell Line
- SHP1 Protein Tyrosine Phosphatase Negatively Modulates Erythroid Differentiation and Suppression of Apoptosis in J2E Erythroleukemic Cells
- Comparative Cleavage Sites within the Reactive-Site Loop of Native and Oxidized α1-Proteinase Inhibitor by Selected Bacterial Proteinases
- A High Affinity Binding Site for the Polypyrimidine Tract Binding Protein (PTB) Is Located in the 5'-Untranslated Region of the Rat Proteinase α1-Inhibitor 3 Variant I Gene
- Defining the Location and Function of Domains of McrB by Deletion Mutagenesis
- Disruption of the Gene for Hsp30, an α-Crystallin-Related Heat Shock Protein of Neurospora crassa, Causes Defects in Import of Proteins into Mitochondria
- Cloning, Purification and Characterisation of Cystathionine γ-Synthase from Nicotiana tabacum
- Isolation and Characterization of Viridin, a New 65 kDa Antifungal Protein from the Mould Trichoderma viride
- The T-Knot Motif Revisited
Articles in the same Issue
- Editors Note
- Walter Neupert: Spellbound by Mitochondria
- Posttranslational Protein Translocation Across the Membrane of the Endoplasmic Reticulum
- Import of Carrier Proteins into Mitochondria
- The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
- Mitochondrial Iron Metabolism in the Yeast Saccharomyces cerevisiae
- A Scj1p Homolog and Folding Catalysts Present in Dog Pancreas Microsomes
- The Import Pathway of Human and Thermoplasma 20S Proteasomes into HeLa Cell Nuclei Is Different from That of Classical NLS-Bearing Proteins
- Role of p52 (NF-kappaB2) in LPS Tolerance in a Human B Cell Line
- SHP1 Protein Tyrosine Phosphatase Negatively Modulates Erythroid Differentiation and Suppression of Apoptosis in J2E Erythroleukemic Cells
- Comparative Cleavage Sites within the Reactive-Site Loop of Native and Oxidized α1-Proteinase Inhibitor by Selected Bacterial Proteinases
- A High Affinity Binding Site for the Polypyrimidine Tract Binding Protein (PTB) Is Located in the 5'-Untranslated Region of the Rat Proteinase α1-Inhibitor 3 Variant I Gene
- Defining the Location and Function of Domains of McrB by Deletion Mutagenesis
- Disruption of the Gene for Hsp30, an α-Crystallin-Related Heat Shock Protein of Neurospora crassa, Causes Defects in Import of Proteins into Mitochondria
- Cloning, Purification and Characterisation of Cystathionine γ-Synthase from Nicotiana tabacum
- Isolation and Characterization of Viridin, a New 65 kDa Antifungal Protein from the Mould Trichoderma viride
- The T-Knot Motif Revisited
