Nucleocytoplasmic transport: the last 200 nanometers

Article Abstract:

The structure and composition of nuclear protein complexes (NPC) are characterized by complexes and signals that are translocated via receptor-mediated interactions. NPC structure retains an 8-fold symmetrical spoke structure and incorporates the basic aspects of conserved membrane-spanning parts. Substrates are relocated in the nucleus or out of it by regulators that stimulate a small GTPase called Ran to hydrolyze GTP, release the resultant GDP and rebind GTP. Moreover, nucleoporins aid in translocating substrates from one extreme of the NPC to the other.

Analysis, Proteins, Cell nuclei, Cell nucleus, Protein conformation

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CRM1 is an export receptor for leucine-rich nuclear export signals

Article Abstract:

CRM1 is distantly related to nuclear protein import mediating receptors, and is also observed to interact with the nuclear pore complex. CRM1 overexpression in Xenopus oocytes stimulates Rev and U snRNA export from the nucleas. Leptomycin B, was found to bind to CRM1 protein, inhibiting nuclear export. CRM1 was found to form a leptomycin B-sensitive complex in vitro, and it is concluded that CRM1 is an export receptor for leucine-rich nuclear export signals.

Observations, Protein binding, Leucine

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Luc7p, a novel yeast U1 snRNP protein with a role in 5' splice site recognition

Article Abstract:

Luc7p, a novel yeast U1 snRNP protein, and its characterization are discussed. The protein has a role in 5' splice site recognition. LUC7 (ital) is an essential gene. Luc7p is necessary for commitment complex formation in vitro. In the presence of a temperature-sensitive type of Luc7p, the protein composition of U1 snRNP, which interacts with the 5' splice site, is changed.

United States, Germany, Statistical Data Included, Research, Genetic aspects, Genetic engineering, Cytochemistry, Yeast, Yeast (Food product), Messenger RNA

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