Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/15397

TitleEfficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin.
Author(s)Chaves, S. R.
Rosenblum, Jonathan S.
KeywordsNuclear transport
Yeast
Issue date9-Feb-2011
PublisherPublic Library of Science
JournalPLoS ONE
Abstract(s)The Karyopherin (Kap) family of nuclear transport receptors enables trafficking of proteins to and from the nucleus in a precise, regulated manner. Individual members function in overlapping pathways, while simultaneously being very specific for their main cargoes. The details of this apparent contradiction and rules governing pathway preference remain to be further elucidated. S. cerevisiae Lhp1 is an abundant protein that functions as an RNA chaperone in a variety of biologically important processes. It localizes almost exclusively to the nucleus and is imported by Kap108. We show that mutation of 3 of the 275 residues in Lhp1 alters its import pathway to a Kap121-dependent process. This mutant does not retain wild-type function and is bound by several chaperones. We propose that Kap121 also acts as a chaperone, one that can act as a genetic buffer by transporting mutated proteins to the nucleus.
TypeArticle
URIhttp://hdl.handle.net/1822/15397
DOI10.1371/journal.pone.0016846
ISSN1932-6203
Publisher versionhttp://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0016846
Peer-Reviewedyes
AccessOpen access
Appears in Collections:DBio - Artigos/Papers

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