Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1990-9-20
pubmed:abstractText
Many RNA-associated proteins contain a ribonucleoprotein (RNP) consensus octamer encompassed by a conserved 80 amino acid sequence, which we have termed an RNA recognition motif (RRM). RRM family members contain either one (class I) or multiple (class II) copies of this motif. We report here that a class II component of the U1 small nuclear RNP (snRNP), the A protein of U1 snRNP (U1snRNP-A), contains two RRMs (RRM1 and -2), yet has only one binding domain (RRM1) that interacts specifically with stem-loop II of U1 RNA. Quantitative analysis of binding affinities of fragments of U1snRNP-A demonstrated that an 86-amino acid polypeptide was competent to bind to U1 RNA with an affinity comparable to that of the full-length protein (Kd approximately 80 nM). The carboxyl-terminal RRM2 of U1snRNP-A did not bind to U1 RNA and may recognize an unidentified heterologous RNA. We propose that class II proteins may function as bridges between RNA components of RNP complexes such as the spliceosome.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2447078, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2453054, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2467746, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2470643, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2505080, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2528681, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2529425, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2531275, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2531658, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2532301, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2620068, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2830282, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2951739, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-2962859, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3028775, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3110598, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3144044, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3144435, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-316537, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3313012, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3315856, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3470736, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3537727, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3856888, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-3907851, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-4573844, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6091052, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6163133, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6219389, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6275366, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6313210, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-6347247, http://linkedlifedata.com/resource/pubmed/commentcorrection/1696729-7029472
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6393-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA.
pubmed:affiliation
Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.
pubmed:publicationType
Journal Article