Role of the Nuclear Transport Factor p10 in Nuclear Import

• Published in: Science (American Association for the Advancement of Science) Vol. 272; no. 5258; pp. 120 - 122
• Main Authors: Nehrbass, Ulf, Blobel, Günter
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 05.04.1996; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: alpha Karyopherins; beta Karyopherins; Biological and medical sciences; Biological Transport, Active; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell Nucleus - metabolism; Cell physiology; Cellular biology; Cloning, Molecular; Fundamental and applied biological sciences. Psychology; Gels; GTP-Binding Proteins - metabolism; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - metabolism; Karyopherins; Liquid phases; Membrane and intracellular transports; Molecular and cellular biology; Molecular Sequence Data; Moorings; Nuclear Envelope - metabolism; Nuclear pore complex proteins; Nuclear Proteins - metabolism; Nucleocytoplasmic Transport Proteins; Polymerase chain reaction; Protein binding; ran GTP-Binding Protein; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins; Silver; Yeasts; Yeast; Import; Enzyme; Triphosphoric monoester hydrolases; Cell nucleus; dGTPase; Esterases; Fungi; Proteins; Membrane transport; Hydrolases; Ascomycetes; Molecular complex; Nucleocytoplasmic transport; Saccharomyces cerevisiae; Nuclear protein; Thallophyta
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.272.5258.120

The nuclear import factor p10 was cloned from Saccharomyces cerevisiae and found to be essential. The protein p10 can bind directly to several peptide repeat-containing nucleoporins. It also binds to the guanosine triphosphatase (GTPase) Ran in its guanosine diphosphate (GDP)-bound form and to karyopherin β. Assembly of the karyopherin heterodimer on immobilized nucleoporin yielded cooperative binding of p10 and Ran-GDP. Addition of GTP to this pentameric complex led to dissociation of karyopherin α, presumably via in situ formation of Ran-GTP from Ran-GDP. Thus, p10 appears to coordinate the Ran-dependent association and dissociation reactions underlying nuclear import.