Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1996-11-13
pubmed:databankReference
pubmed:abstractText
The essential eukaryotic pre-mRNA splicing factor U2AF (U2 small nuclear ribonucleoprotein auxiliary factor) is required to specify the 3' splice at an early step in spliceosome assembly. U2AF binds site-specifically to the intron polypyrimidine tract and recruits U2 small nuclear ribonucleoprotein to the branch site. Human U2AF (hU2AF) is a heterodimer composed of a large (hU2AF65) and small (hU2AF35) subunit. Although these proteins associate in a tight complex, the biochemical requirement for U2AF activity can be satisfied solely by the large subunit. The requirement for the small subunit in splicing has remained enigmatic. No biochemical activity has been found for hU2AF35 and it has been implicated in splicing only indirectly by its interaction with known splicing factors. In the absence of a biochemical assay, we have taken a genetic approach to investigate the function of the small subunit in the fruit fly Drosophila melanogaster. A cDNA clone encoding the small subunit of Drosophila U2AF (dU2AF38) has been isolated and sequenced. The dU2AF38 protein is highly homologous to hU2AF35 containing a conserved central arginine- and serine-rich (RS) domain. A recessive P-element insertion mutation affecting dU2AF38 causes a reduction in viability and fertility and morphological bristle defects. Consistent with a general role in splicing, a null allele of dU2AF38 is fully penetrant recessive lethal, like null alleles of the Drosophila U2AF large subunit.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-1388271, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-1538748, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-1824937, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-1839712, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-1853200, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2164887, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2453394, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2473007, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2505080, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2628164, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-2963698, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-3097509, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-3199441, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-6176879, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-7565780, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-7692602, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-7867926, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-7935465, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-7958851, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8035814, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8211184, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8261509, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8290338, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8334698, http://linkedlifedata.com/resource/pubmed/commentcorrection/8816800-8647433
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10333-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:8816800-Alleles, pubmed-meshheading:8816800-Amino Acid Sequence, pubmed-meshheading:8816800-Animals, pubmed-meshheading:8816800-Animals, Genetically Modified, pubmed-meshheading:8816800-DNA Transposable Elements, pubmed-meshheading:8816800-Drosophila melanogaster, pubmed-meshheading:8816800-Female, pubmed-meshheading:8816800-Genes, Insect, pubmed-meshheading:8816800-Genes, Lethal, pubmed-meshheading:8816800-Genetic Complementation Test, pubmed-meshheading:8816800-Humans, pubmed-meshheading:8816800-Male, pubmed-meshheading:8816800-Molecular Sequence Data, pubmed-meshheading:8816800-Mutagenesis, pubmed-meshheading:8816800-Nuclear Proteins, pubmed-meshheading:8816800-RNA Precursors, pubmed-meshheading:8816800-RNA Splicing, pubmed-meshheading:8816800-Ribonucleoproteins, pubmed-meshheading:8816800-Sequence Deletion, pubmed-meshheading:8816800-Sequence Homology, Amino Acid
pubmed:year
1996
pubmed:articleTitle
Mutations in the small subunit of the Drosophila U2AF splicing factor cause lethality and developmental defects.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't