Eintrag weiter verarbeiten
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome
Gespeichert in:
| Zeitschriftentitel: | RNA |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , |
| In: | RNA, 22, 2016, 2, S. 265-277 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. |
|---|---|
| author |
Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. |
| spellingShingle |
Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. RNA Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome Molecular Biology |
| author_sort |
schütze, tonio |
| spelling |
Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.054296.115 <jats:p>Spliceosomal Prp38 proteins contain a conserved amino-terminal domain, but only higher eukaryotic orthologs also harbor a carboxy-terminal RS domain, a hallmark of splicing regulatory SR proteins. We show by crystal structure analysis that the amino-terminal domain of human Prp38 is organized around three pairs of antiparallel α-helices and lacks similarities to RNA-binding domains found in canonical SR proteins. Instead, yeast two-hybrid analyses suggest that the amino-terminal domain is a versatile protein–protein interaction hub that possibly binds 12 other spliceosomal proteins, most of which are recruited at the same stage as Prp38. By quantitative, alanine surface-scanning two-hybrid screens and biochemical analyses we delineated four distinct interfaces on the Prp38 amino-terminal domain. In vitro interaction assays using recombinant proteins showed that Prp38 can bind at least two proteins simultaneously via two different interfaces. Addition of excess Prp38 amino-terminal domain to in vitro splicing assays, but not of an interaction-deficient mutant, stalled splicing at a precatalytic stage. Our results show that human Prp38 is an unusual SR protein, whose amino-terminal domain is a multi-interface protein–protein interaction platform that might organize the relative positioning of other proteins during splicing.</jats:p> Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome RNA |
| doi_str_mv |
10.1261/rna.054296.115 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMDU0Mjk2LjExNQ |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMDU0Mjk2LjExNQ |
| institution |
DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 |
| imprint |
Cold Spring Harbor Laboratory, 2016 |
| imprint_str_mv |
Cold Spring Harbor Laboratory, 2016 |
| issn |
1355-8382 1469-9001 |
| issn_str_mv |
1355-8382 1469-9001 |
| language |
English |
| mega_collection |
Cold Spring Harbor Laboratory (CrossRef) |
| match_str |
schutze2016multipleproteinproteininteractionsconvergingontheprp38proteinduringactivationofthehumanspliceosome |
| publishDateSort |
2016 |
| publisher |
Cold Spring Harbor Laboratory |
| recordtype |
ai |
| record_format |
ai |
| series |
RNA |
| source_id |
49 |
| title |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_unstemmed |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_full |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_fullStr |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_full_unstemmed |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_short |
Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_sort |
multiple protein–protein interactions converging on the prp38 protein during activation of the human spliceosome |
| topic |
Molecular Biology |
| url |
http://dx.doi.org/10.1261/rna.054296.115 |
| publishDate |
2016 |
| physical |
265-277 |
| description |
<jats:p>Spliceosomal Prp38 proteins contain a conserved amino-terminal domain, but only higher eukaryotic orthologs also harbor a carboxy-terminal RS domain, a hallmark of splicing regulatory SR proteins. We show by crystal structure analysis that the amino-terminal domain of human Prp38 is organized around three pairs of antiparallel α-helices and lacks similarities to RNA-binding domains found in canonical SR proteins. Instead, yeast two-hybrid analyses suggest that the amino-terminal domain is a versatile protein–protein interaction hub that possibly binds 12 other spliceosomal proteins, most of which are recruited at the same stage as Prp38. By quantitative, alanine surface-scanning two-hybrid screens and biochemical analyses we delineated four distinct interfaces on the Prp38 amino-terminal domain. In vitro interaction assays using recombinant proteins showed that Prp38 can bind at least two proteins simultaneously via two different interfaces. Addition of excess Prp38 amino-terminal domain to in vitro splicing assays, but not of an interaction-deficient mutant, stalled splicing at a precatalytic stage. Our results show that human Prp38 is an unusual SR protein, whose amino-terminal domain is a multi-interface protein–protein interaction platform that might organize the relative positioning of other proteins during splicing.</jats:p> |
| container_issue |
2 |
| container_start_page |
265 |
| container_title |
RNA |
| container_volume |
22 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792344586189799429 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T17:07:25.009Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Multiple+protein%E2%80%93protein+interactions+converging+on+the+Prp38+protein+during+activation+of+the+human+spliceosome&rft.date=2016-02-01&genre=article&issn=1469-9001&volume=22&issue=2&spage=265&epage=277&pages=265-277&jtitle=RNA&atitle=Multiple+protein%E2%80%93protein+interactions+converging+on+the+Prp38+protein+during+activation+of+the+human+spliceosome&aulast=Wahl&aufirst=Markus+C.&rft_id=info%3Adoi%2F10.1261%2Frna.054296.115&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792344586189799429 |
| author | Schütze, Tonio, Ulrich, Alexander K.C., Apelt, Luise, Will, Cindy L., Bartlick, Natascha, Seeger, Martin, Weber, Gert, Lührmann, Reinhard, Stelzl, Ulrich, Wahl, Markus C. |
| author_facet | Schütze, Tonio, Ulrich, Alexander K.C., Apelt, Luise, Will, Cindy L., Bartlick, Natascha, Seeger, Martin, Weber, Gert, Lührmann, Reinhard, Stelzl, Ulrich, Wahl, Markus C., Schütze, Tonio, Ulrich, Alexander K.C., Apelt, Luise, Will, Cindy L., Bartlick, Natascha, Seeger, Martin, Weber, Gert, Lührmann, Reinhard, Stelzl, Ulrich, Wahl, Markus C. |
| author_sort | schütze, tonio |
| container_issue | 2 |
| container_start_page | 265 |
| container_title | RNA |
| container_volume | 22 |
| description | <jats:p>Spliceosomal Prp38 proteins contain a conserved amino-terminal domain, but only higher eukaryotic orthologs also harbor a carboxy-terminal RS domain, a hallmark of splicing regulatory SR proteins. We show by crystal structure analysis that the amino-terminal domain of human Prp38 is organized around three pairs of antiparallel α-helices and lacks similarities to RNA-binding domains found in canonical SR proteins. Instead, yeast two-hybrid analyses suggest that the amino-terminal domain is a versatile protein–protein interaction hub that possibly binds 12 other spliceosomal proteins, most of which are recruited at the same stage as Prp38. By quantitative, alanine surface-scanning two-hybrid screens and biochemical analyses we delineated four distinct interfaces on the Prp38 amino-terminal domain. In vitro interaction assays using recombinant proteins showed that Prp38 can bind at least two proteins simultaneously via two different interfaces. Addition of excess Prp38 amino-terminal domain to in vitro splicing assays, but not of an interaction-deficient mutant, stalled splicing at a precatalytic stage. Our results show that human Prp38 is an unusual SR protein, whose amino-terminal domain is a multi-interface protein–protein interaction platform that might organize the relative positioning of other proteins during splicing.</jats:p> |
| doi_str_mv | 10.1261/rna.054296.115 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI2MS9ybmEuMDU0Mjk2LjExNQ |
| imprint | Cold Spring Harbor Laboratory, 2016 |
| imprint_str_mv | Cold Spring Harbor Laboratory, 2016 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
| issn | 1355-8382, 1469-9001 |
| issn_str_mv | 1355-8382, 1469-9001 |
| language | English |
| last_indexed | 2024-03-01T17:07:25.009Z |
| match_str | schutze2016multipleproteinproteininteractionsconvergingontheprp38proteinduringactivationofthehumanspliceosome |
| mega_collection | Cold Spring Harbor Laboratory (CrossRef) |
| physical | 265-277 |
| publishDate | 2016 |
| publishDateSort | 2016 |
| publisher | Cold Spring Harbor Laboratory |
| record_format | ai |
| recordtype | ai |
| series | RNA |
| source_id | 49 |
| spelling | Schütze, Tonio Ulrich, Alexander K.C. Apelt, Luise Will, Cindy L. Bartlick, Natascha Seeger, Martin Weber, Gert Lührmann, Reinhard Stelzl, Ulrich Wahl, Markus C. 1355-8382 1469-9001 Cold Spring Harbor Laboratory Molecular Biology http://dx.doi.org/10.1261/rna.054296.115 <jats:p>Spliceosomal Prp38 proteins contain a conserved amino-terminal domain, but only higher eukaryotic orthologs also harbor a carboxy-terminal RS domain, a hallmark of splicing regulatory SR proteins. We show by crystal structure analysis that the amino-terminal domain of human Prp38 is organized around three pairs of antiparallel α-helices and lacks similarities to RNA-binding domains found in canonical SR proteins. Instead, yeast two-hybrid analyses suggest that the amino-terminal domain is a versatile protein–protein interaction hub that possibly binds 12 other spliceosomal proteins, most of which are recruited at the same stage as Prp38. By quantitative, alanine surface-scanning two-hybrid screens and biochemical analyses we delineated four distinct interfaces on the Prp38 amino-terminal domain. In vitro interaction assays using recombinant proteins showed that Prp38 can bind at least two proteins simultaneously via two different interfaces. Addition of excess Prp38 amino-terminal domain to in vitro splicing assays, but not of an interaction-deficient mutant, stalled splicing at a precatalytic stage. Our results show that human Prp38 is an unusual SR protein, whose amino-terminal domain is a multi-interface protein–protein interaction platform that might organize the relative positioning of other proteins during splicing.</jats:p> Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome RNA |
| spellingShingle | Schütze, Tonio, Ulrich, Alexander K.C., Apelt, Luise, Will, Cindy L., Bartlick, Natascha, Seeger, Martin, Weber, Gert, Lührmann, Reinhard, Stelzl, Ulrich, Wahl, Markus C., RNA, Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome, Molecular Biology |
| title | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_full | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_fullStr | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_full_unstemmed | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_short | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| title_sort | multiple protein–protein interactions converging on the prp38 protein during activation of the human spliceosome |
| title_unstemmed | Multiple protein–protein interactions converging on the Prp38 protein during activation of the human spliceosome |
| topic | Molecular Biology |
| url | http://dx.doi.org/10.1261/rna.054296.115 |