Recombinant hnRNP protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites.
Identifieur interne : 002A15 ( PubMed/Corpus ); précédent : 002A14; suivant : 002A16Recombinant hnRNP protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites.
Auteurs : M. Buvoli ; F. Cobianchi ; G. Biamonti ; S. RivaSource :
- Nucleic acids research [ 0305-1048 ] ; 1990.
English descriptors
- KwdEn :
- Base Sequence, Binding, Competitive, Exons, Globins (genetics), Heterogeneous Nuclear Ribonucleoprotein A1, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Heterogeneous-Nuclear Ribonucleoproteins, Humans, Introns, Molecular Sequence Data, Oligodeoxyribonucleotides (chemistry), RNA Precursors (chemistry), RNA Splicing, Recombinant Proteins (metabolism), Ribonucleoproteins (metabolism), Sequence Homology, Nucleic Acid.
- MESH :
- chemical , chemistry : Oligodeoxyribonucleotides, RNA Precursors.
- chemical , genetics : Globins.
- chemical , metabolism : Recombinant Proteins, Ribonucleoproteins.
- Base Sequence, Binding, Competitive, Exons, Heterogeneous Nuclear Ribonucleoprotein A1, Heterogeneous-Nuclear Ribonucleoprotein Group A-B, Heterogeneous-Nuclear Ribonucleoproteins, Humans, Introns, Molecular Sequence Data, RNA Splicing, Sequence Homology, Nucleic Acid.
Abstract
The reported binding preference of human hnRNP protein A1 for the 3'-splice site of some introns (Swanson and Dreyfuss (1988) EMBO J. 7, 3519-3529; Mayrand and Pederson (1990) Nucleic Acids Res. 18, 3307-3318) was tested by assaying in vitro the binding of purified recombinant A1 protein (expressed in bacteria) to synthetic oligodeoxynucleotides (21-mers) of suitable sequence. In such a minimal system we find preferential binding of protein A1 to oligodeoxynucleotide sequences corresponding to the 3'-splice site of IVS1 of human beta-globin pre-mRNA and of IVS1 of Adenovirus type 2 major late transcript. Mutation studies demonstrate that the binding specificity is dependent on the known critical domains of this intron region, the AG splice site dinucleotide and polypyrimidine tract, and resides entirely in the short oligonucleotide sequence. Moreover specific binding does not require the presence of other hnRNP proteins or of snRNP particles. Studies with a truncated recombinant protein demonstrated that the minimal protein sequence determinants for A1 recognition of 3'-splice acceptor site reside entirely in the N-terminal 195 aa of the unmodified protein.
DOI: 10.1093/nar/18.22.6595
PubMed: 2251120
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pubmed:2251120Le document en format XML
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Riva</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1990">1990</date><idno type="RBID">pubmed:2251120</idno><idno type="pmid">2251120</idno><idno type="doi">10.1093/nar/18.22.6595</idno><idno type="wicri:Area/PubMed/Corpus">002A15</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A15</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Recombinant hnRNP protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites.</title><author><name sortKey="Buvoli, M" sort="Buvoli, M" uniqKey="Buvoli M" first="M" last="Buvoli">M. Buvoli</name><affiliation><nlm:affiliation>Istituto di Genetica Biochimica ed Evoluzionistica, Pavia, Italy.</nlm:affiliation></affiliation></author><author><name sortKey="Cobianchi, F" sort="Cobianchi, F" uniqKey="Cobianchi F" first="F" last="Cobianchi">F. Cobianchi</name></author><author><name sortKey="Biamonti, G" sort="Biamonti, G" uniqKey="Biamonti G" first="G" last="Biamonti">G. Biamonti</name></author><author><name sortKey="Riva, S" sort="Riva, S" uniqKey="Riva S" first="S" last="Riva">S. Riva</name></author></analytic><series><title level="j">Nucleic acids research</title><idno type="ISSN">0305-1048</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term><term>Binding, Competitive</term><term>Exons</term><term>Globins (genetics)</term><term>Heterogeneous Nuclear Ribonucleoprotein A1</term><term>Heterogeneous-Nuclear Ribonucleoprotein Group A-B</term><term>Heterogeneous-Nuclear Ribonucleoproteins</term><term>Humans</term><term>Introns</term><term>Molecular Sequence Data</term><term>Oligodeoxyribonucleotides (chemistry)</term><term>RNA Precursors (chemistry)</term><term>RNA Splicing</term><term>Recombinant Proteins (metabolism)</term><term>Ribonucleoproteins (metabolism)</term><term>Sequence Homology, Nucleic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oligodeoxyribonucleotides</term><term>RNA Precursors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Globins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term><term>Ribonucleoproteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Binding, Competitive</term><term>Exons</term><term>Heterogeneous Nuclear Ribonucleoprotein A1</term><term>Heterogeneous-Nuclear Ribonucleoprotein Group A-B</term><term>Heterogeneous-Nuclear Ribonucleoproteins</term><term>Humans</term><term>Introns</term><term>Molecular Sequence Data</term><term>RNA Splicing</term><term>Sequence Homology, Nucleic Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The reported binding preference of human hnRNP protein A1 for the 3'-splice site of some introns (Swanson and Dreyfuss (1988) EMBO J. 7, 3519-3529; Mayrand and Pederson (1990) Nucleic Acids Res. 18, 3307-3318) was tested by assaying in vitro the binding of purified recombinant A1 protein (expressed in bacteria) to synthetic oligodeoxynucleotides (21-mers) of suitable sequence. In such a minimal system we find preferential binding of protein A1 to oligodeoxynucleotide sequences corresponding to the 3'-splice site of IVS1 of human beta-globin pre-mRNA and of IVS1 of Adenovirus type 2 major late transcript. Mutation studies demonstrate that the binding specificity is dependent on the known critical domains of this intron region, the AG splice site dinucleotide and polypyrimidine tract, and resides entirely in the short oligonucleotide sequence. Moreover specific binding does not require the presence of other hnRNP proteins or of snRNP particles. Studies with a truncated recombinant protein demonstrated that the minimal protein sequence determinants for A1 recognition of 3'-splice acceptor site reside entirely in the N-terminal 195 aa of the unmodified protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2251120</PMID><DateCompleted><Year>1991</Year><Month>01</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0305-1048</ISSN><JournalIssue CitedMedium="Print"><Volume>18</Volume><Issue>22</Issue><PubDate><Year>1990</Year><Month>Nov</Month><Day>25</Day></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>Recombinant hnRNP protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites.</ArticleTitle><Pagination><MedlinePgn>6595-600</MedlinePgn></Pagination><Abstract><AbstractText>The reported binding preference of human hnRNP protein A1 for the 3'-splice site of some introns (Swanson and Dreyfuss (1988) EMBO J. 7, 3519-3529; Mayrand and Pederson (1990) Nucleic Acids Res. 18, 3307-3318) was tested by assaying in vitro the binding of purified recombinant A1 protein (expressed in bacteria) to synthetic oligodeoxynucleotides (21-mers) of suitable sequence. In such a minimal system we find preferential binding of protein A1 to oligodeoxynucleotide sequences corresponding to the 3'-splice site of IVS1 of human beta-globin pre-mRNA and of IVS1 of Adenovirus type 2 major late transcript. Mutation studies demonstrate that the binding specificity is dependent on the known critical domains of this intron region, the AG splice site dinucleotide and polypyrimidine tract, and resides entirely in the short oligonucleotide sequence. Moreover specific binding does not require the presence of other hnRNP proteins or of snRNP particles. Studies with a truncated recombinant protein demonstrated that the minimal protein sequence determinants for A1 recognition of 3'-splice acceptor site reside entirely in the N-terminal 195 aa of the unmodified protein.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Buvoli</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Istituto di Genetica Biochimica ed Evoluzionistica, Pavia, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cobianchi</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Biamonti</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Riva</LastName><ForeName>S</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012261">Ribonucleoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-22-2</RegistryNumber><NameOfSubstance UI="D005914">Globins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001667" MajorTopicYN="N">Binding, Competitive</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005091" MajorTopicYN="Y">Exons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005914" MajorTopicYN="N">Globins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076245" MajorTopicYN="N">Heterogeneous Nuclear Ribonucleoprotein 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PubStatus="entrez"><Year>1990</Year><Month>11</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">2251120</ArticleId><ArticleId IdType="pmc">PMC332615</ArticleId><ArticleId IdType="doi">10.1093/nar/18.22.6595</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 1976 Apr 10;251(7):2124-32</Citation><ArticleIdList><ArticleId IdType="pubmed">1270425</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1990 Jun 11;18(11):3307-18</Citation><ArticleIdList><ArticleId IdType="pubmed">2141400</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1981 Jan 5;145(1):75-104</Citation><ArticleIdList><ArticleId IdType="pubmed">7265204</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1983 Mar;80(6):1599-602</Citation><ArticleIdList><ArticleId IdType="pubmed">6572923</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1983 Jul;97(1):99-111</Citation><ArticleIdList><ArticleId IdType="pubmed">6134739</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1983 Sep 13;22(19):4592-600</Citation><ArticleIdList><ArticleId IdType="pubmed">6626517</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1983 Dec 25;171(4):439-55</Citation><ArticleIdList><ArticleId IdType="pubmed">6319710</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1984 Apr;36(4):993-1005</Citation><ArticleIdList><ArticleId IdType="pubmed">6323033</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1984 Sep 10;259(17):10850-6</Citation><ArticleIdList><ArticleId IdType="pubmed">6540775</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1984 Aug 31;225(4665):898-903</Citation><ArticleIdList><ArticleId IdType="pubmed">6206566</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1985 Nov;43(1):143-51</Citation><ArticleIdList><ArticleId IdType="pubmed">3935315</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1986 Jan 15;261(2):878-83</Citation><ArticleIdList><ArticleId IdType="pubmed">3941105</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1986 Mar 15;261(8):3512-8</Citation><ArticleIdList><ArticleId IdType="pubmed">3949776</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1986 Mar 15;261(8):3536-43</Citation><ArticleIdList><ArticleId IdType="pubmed">3005291</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1986 Mar 28;231(4745):1534-9</Citation><ArticleIdList><ArticleId IdType="pubmed">3952495</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1986 Jul 11;14(13):5241-54</Citation><ArticleIdList><ArticleId IdType="pubmed">3737400</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1986 Dec 5;47(5):755-66</Citation><ArticleIdList><ArticleId IdType="pubmed">2946417</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1986 Dec 26;47(6):973-84</Citation><ArticleIdList><ArticleId IdType="pubmed">2946421</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1986 Sep;5(9):2267-73</Citation><ArticleIdList><ArticleId IdType="pubmed">3023065</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Cell Biol. 1986;2:459-98</Citation><ArticleIdList><ArticleId IdType="pubmed">3548774</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1988 Jan 15;263(2):1063-71</Citation><ArticleIdList><ArticleId IdType="pubmed">2447078</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1988 Mar 5;263(7):3307-13</Citation><ArticleIdList><ArticleId IdType="pubmed">2830282</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteins. 1986 Nov;1(3):195-210</Citation><ArticleIdList><ArticleId IdType="pubmed">3329728</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1988 May 11;16(9):3751-70</Citation><ArticleIdList><ArticleId IdType="pubmed">2836799</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1988 May;8(5):2237-41</Citation><ArticleIdList><ArticleId IdType="pubmed">3386636</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1988 Jul;8(7):2884-95</Citation><ArticleIdList><ArticleId IdType="pubmed">3405221</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1988 Sep 2;241(4870):1182-7</Citation><ArticleIdList><ArticleId IdType="pubmed">2842864</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1988 Nov;7(11):3519-29</Citation><ArticleIdList><ArticleId IdType="pubmed">3208740</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1989 Apr 7;57(1):89-101</Citation><ArticleIdList><ArticleId IdType="pubmed">2467746</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biochem Sci. 1988 Mar;13(3):86-91</Citation><ArticleIdList><ArticleId IdType="pubmed">3072706</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1989 Apr;3(4):431-7</Citation><ArticleIdList><ArticleId IdType="pubmed">2470643</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1989 Jun 5;207(3):491-503</Citation><ArticleIdList><ArticleId IdType="pubmed">2760922</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1989 Sep 25;17(18):7333-44</Citation><ArticleIdList><ArticleId IdType="pubmed">2798095</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1989 Oct;3(10):1562-71</Citation><ArticleIdList><ArticleId IdType="pubmed">2612905</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1989 Dec;3(12A):1874-86</Citation><ArticleIdList><ArticleId IdType="pubmed">2533575</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1990 Apr;9(4):1229-35</Citation><ArticleIdList><ArticleId IdType="pubmed">1691095</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1990 Jun 7;345(6275):502-6</Citation><ArticleIdList><ArticleId IdType="pubmed">2140872</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1980 May;20(1):75-84</Citation><ArticleIdList><ArticleId IdType="pubmed">6771017</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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