10428841

Source:http://linkedlifedata.com/resource/pubmed/id/10428841

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0032098, umls-concept:C0086597, umls-concept:C0162326, umls-concept:C0292147, umls-concept:C0299508, umls-concept:C0332291, umls-concept:C0475264, umls-concept:C0521447, umls-concept:C0887839, umls-concept:C1145667, umls-concept:C1510827, umls-concept:C2003941
pubmed:issue	32
pubmed:dateCreated	1999-9-2
pubmed:abstractText	Nuclear import of conventional nuclear localization sequence (NLS)-containing proteins initially involves recognition by the importin (IMP) alpha/beta heterodimer, where IMPalpha binds the NLS and IMPbeta targets the IMPalpha/NLS-containing protein complex to the nuclear pore. Here we examine IMPalpha from the plant Arabidopsis thaliana (At-IMPalpha), which exhibits nuclear envelope localization typical of IMPbeta rather than IMPalpha in other eukaryotic cell systems. We show that At-IMPalpha recognizes conventional NLSs of two different types with high affinity (K(d) of 5-10 nM), in contrast to mouse IMPalpha (m-IMPalpha), which exhibits much lower affinity (K(d) of 50-70 nM) and only achieves high affinity in the presence of m-IMPbeta. Unlike m-IMPalpha, At-IMPalpha is thus a high affinity NLS receptor in the absence of IMPbeta. Interestingly, At-IMPalpha was also able to bind with high affinity to NLSs recognized specifically by m-IMPbeta and not m-IMPalpha, including that of the maize transcription factor Opaque-2. Reconstitution of nuclear import in vitro indicated that in the absence of exogenous IMPbeta subunit but dependent on RanGDP and NTF2, At-IMPalpha was able to mediate nuclear accumulation to levels comparable with those mediated by m-IMPalpha/beta. Neither m-IMPalpha nor -beta was able to mediate nuclear import in the absence of the other subunit. At-IMPalpha's novel NLS recognition and nuclear transport properties imply that plants may possess an IMPalpha-mediated nuclear import pathway independent of IMPbeta in addition to that mediated by IMPalpha/beta.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nutf2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/opaque-2 protein, Zea mays, http://linkedlifedata.com/resource/pubmed/chemical/ran GTP-Binding Protein
pubmed:status	MEDLINE
pubmed:month	Aug
pubmed:issn	0021-9258
pubmed:author	pubmed-author:ChanC KCK, pubmed-author:HübnerSS, pubmed-author:HuWW, pubmed-author:JansD ADA, pubmed-author:PaschalB MBM, pubmed-author:RaikhelN VNV, pubmed-author:RihsH PHP, pubmed-author:SmithH MHM
pubmed:issnType	Print
pubmed:day	6
pubmed:volume	274
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	22610-7
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:10428841-Amino Acid Sequence, pubmed-meshheading:10428841-Animals, pubmed-meshheading:10428841-Arabidopsis, pubmed-meshheading:10428841-Biological Transport, pubmed-meshheading:10428841-Carrier Proteins, pubmed-meshheading:10428841-Cell Nucleus, pubmed-meshheading:10428841-DNA-Binding Proteins, pubmed-meshheading:10428841-GTP-Binding Proteins, pubmed-meshheading:10428841-Karyopherins, pubmed-meshheading:10428841-Mice, pubmed-meshheading:10428841-Molecular Sequence Data, pubmed-meshheading:10428841-Nuclear Localization Signals, pubmed-meshheading:10428841-Nuclear Proteins, pubmed-meshheading:10428841-Nucleocytoplasmic Transport Proteins, pubmed-meshheading:10428841-Plant Proteins, pubmed-meshheading:10428841-Protein Binding, pubmed-meshheading:10428841-Recombinant Fusion Proteins, pubmed-meshheading:10428841-Transcription Factors, pubmed-meshheading:10428841-ran GTP-Binding Protein
pubmed:year	1999
pubmed:articleTitle	Plant importin alpha binds nuclear localization sequences with high affinity and can mediate nuclear import independent of importin beta.
pubmed:affiliation	Nuclear Signalling Laboratory, Division for Biochemistry and Molecular Biology, John Curtin School of Medical Research, Canberra ACT 2601, Australia.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.