Affiliation:
1. Medizinische Biochemie und Molekularbiologie, Universität des Saarlandes, D-66421 Homburg, Germany
Abstract
ABSTRACT
The nucleocytoplasmic exchange of macromolecules is mediated by receptors specialized in passage through the nuclear pore complex. The majority of these receptors belong to the importin β protein family, which has 14 members in
Saccharomyces cerevisiae
. Nine importins carry various cargos from the cytoplasm into the nucleus, whereas four exportins mediate nuclear export. Kap120 is the only receptor whose transport cargo has not been found previously. Here, we characterize Kap120 as an importin for the ribosome maturation factor Rpf1, which was identified in a two-hybrid screen. Kap120 binds directly to Rpf1 in vitro and is released by Ran-GTP. At least three parallel import pathways exist for Rpf1, since nuclear import is defective in strains with the importins Kap120, Kap114, and Nmd5 deleted. Both
kap120
and
rpf1
mutants accumulate large ribosomal subunits in the nucleus. The nuclear accumulation of 60S ribosomal subunits in
kap120
mutants is abolished upon
RPF1
overexpression, indicating that Kap120 does not function in the actual ribosomal export step but rather in import of ribosome maturation factors.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
16 articles.
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