Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-3-10
pubmed:abstractText
Mex67p and Mtr2p constitute an essential mRNA export complex that interacts with poly(A)+ RNA and nuclear pore proteins. We have identified Yra1p, an intranuclear protein with in vitro RNA-RNA annealing activity, which directly binds to Mex67p. The complex between Yra1p and Mex67p was reconstituted in vitro and shown by UV-crosslinking to bind directly to RNA. Mutants of YRA1 are impaired in nuclear poly(A)+ RNA export at restrictive growth conditions. ALY, the mouse homologue of Yra1p and a transcriptional coactivator, can bind in vitro to yeast and human Mex67p and partly complements the otherwise non-viable yra1 null mutant. Thus, Yra1p is the first RNA-binding protein characterized, which bridges the shuttling Mex67p/Mtr2p exporter to intranuclear mRNA transport cargoes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10202158, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10228171, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10323864, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10376682, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10393189, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-10395558, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-1464327, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7508381, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7543368, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7762298, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7813444, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7865887, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-7969175, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-8565072, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-8675010, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-8848052, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-8970155, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9056715, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9119228, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9149233, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9214641, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9226715, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9323132, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9334319, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9463388, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9564047, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9564048, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9660949, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9744791, http://linkedlifedata.com/resource/pubmed/commentcorrection/10722314-9774696
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MEX67 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleocytoplasmic Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Poly A, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Refbp1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/THOC4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/YRA1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
410-20
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:10722314-Amino Acid Sequence, pubmed-meshheading:10722314-Animals, pubmed-meshheading:10722314-Biological Transport, pubmed-meshheading:10722314-Fungal Proteins, pubmed-meshheading:10722314-Humans, pubmed-meshheading:10722314-Mice, pubmed-meshheading:10722314-Microscopy, Fluorescence, pubmed-meshheading:10722314-Molecular Sequence Data, pubmed-meshheading:10722314-Mutation, pubmed-meshheading:10722314-Nuclear Proteins, pubmed-meshheading:10722314-Nucleocytoplasmic Transport Proteins, pubmed-meshheading:10722314-Poly A, pubmed-meshheading:10722314-Protein Binding, pubmed-meshheading:10722314-RNA, Messenger, pubmed-meshheading:10722314-RNA-Binding Proteins, pubmed-meshheading:10722314-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10722314-Sequence Homology, Amino Acid, pubmed-meshheading:10722314-Transcription Factors, pubmed-meshheading:10722314-Yeasts
pubmed:year
2000
pubmed:articleTitle
Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export.
pubmed:affiliation
BZH, Biochemie-Zentrum Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't