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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
The identification and localization of a novel form of RanGAP1, a nuclear Ras-like GTPase that is required for the bidirectional transport of proteins and ribnucleoproteins across the nuclear pore complex (NPC), was reported. Expand
Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
It is proposed that movement of NLS proteins across the nuclear pore complex is a stochastic process that operates via repeated association-dissociation reactions. Expand
Crystallographic Analysis of the Recognition of a Nuclear Localization Signal by the Nuclear Import Factor Karyopherin α
The crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha is reported, which reveals the determinants of NLS specificity and suggests a model for the recognition of bipartite NLSs. Expand
Isolation of components of the chloroplast protein import machinery.
Six envelope polypeptides copurified specifically and, apparently, stoichiometrically with the import intermediates of the chloroplast, including a homolog of the heat shock protein hsp70 and a channel-protein candidate. Expand
Preparation of microsomal membranes for cotranslational protein translocation.
Publisher Summary This chapter describes a rapid isolation procedure that reproducibly yields highly active microsomal membranes, and presents method for refining the crude rough microsomes (RM)Expand
A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization.
It is proposed that Mms21 sumoylates proteins involved in these diverse processes and that the other members of the complex, particularly Smc5/6, facilitate proper substrate sumoylation by localizing Mms 21 to specific chromosomal regions. Expand
The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
It is reported that two interacting components are required for full fraction-B activity, purify one of these components to homogeneity, and show that it is the highly abundant GTP-binding protein Ran (Ras-related nuclear protein)/TC4. Expand
The ubiquitin‐like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
Experiments with conditional uba2 mutants showed that Uba2p is required for Smt3p conjugation in vivo, and UBA2 and AOS1 are both essential genes, providing additional evidence that they act in a distinct pathway whose role in cell viability is to conjugate SmT3p to other proteins. Expand
A Distinct Nuclear Import Pathway Used by Ribosomal Proteins
It is shown that the related protein Pse1p is also a karyopherin and can functionally substitute for Kap123p; both are capable of specifically directing a ribosomal nuclear localization signal reporter to the nucleus in vivo. Expand
Nup358, a Cytoplasmically Exposed Nucleoporin with Peptide Repeats, Ran-GTP Binding Sites, Zinc Fingers, a Cyclophilin A Homologous Domain, and a Leucine-rich Region (*)
Nup358 is the first nucleoporin shown to contain binding sites for two of three soluble nuclear transport factors so far isolated, namely karyopherin and Ran-GTP. Expand