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dc.contributor.author
Kuwasako, Kanako
dc.contributor.author
Nameki, Nobukazu
dc.contributor.author
Tsuda, Kengo
dc.contributor.author
Takahashi, Mari
dc.contributor.author
Sato, Atsuko
dc.contributor.author
Tochio, Naoya
dc.contributor.author
Inoue, Makoto
dc.contributor.author
Terada, Takaho
dc.contributor.author
Kigawa, Takanori
dc.contributor.author
Kobayashi, Naohiro
dc.contributor.author
Shirouzu, Mikako
dc.contributor.author
Ito, Takuhiro
dc.contributor.author
Sakamoto, Taiichi
dc.contributor.author
Wakamatsu, Kaori
dc.contributor.author
Guntert, Peter
dc.contributor.author
Takahashi, Seizo
dc.contributor.author
Yokoyama, Shigeyuki
dc.contributor.author
Muto, Yutaka
dc.date.accessioned
2017-07-18T14:57:47Z
dc.date.available
2017-06-12T18:07:15Z
dc.date.available
2017-07-18T14:57:47Z
dc.date.issued
2017-02
dc.identifier.issn
0961-8368
dc.identifier.issn
1469-896X
dc.identifier.other
10.1002/pro.3080
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/125494
dc.identifier.doi
10.3929/ethz-b-000125494
dc.description.abstract
The spliceosomal protein SF3b49, a component of the splicing factor 3b (SF3b) protein complex in the U2 small nuclear ribonucleoprotein, contains two RNA recognition motif (RRM) domains. In yeast, the first RRM domain (RRM1) of Hsh49 protein (yeast orthologue of human SF3b49) reportedly interacts with another component, Cus1 protein (orthologue of human SF3b145). Here, we solved the solution structure of the RRM1 of human SF3b49 and examined its mode of interaction with a fragment of human SF3b145 using NMR methods. Chemical shift mapping showed that the SF3b145 fragment spanning residues 598–631 interacts with SF3b49 RRM1, which adopts a canonical RRM fold with a topology of β1-α1-β2-β3-α2-β4. Furthermore, a docking model based on NOESY measurements suggests that residues 607–616 of the SF3b145 fragment adopt a helical structure that binds to RRM1 predominantly via α1, consequently exhibiting a helix–helix interaction in almost antiparallel. This mode of interaction was confirmed by a mutational analysis using GST pull-down assays. Comparison with structures of all RRM domains when complexed with a peptide found that this helix–helix interaction is unique to SF3b49 RRM1. Additionally, all amino acid residues involved in the interaction are well conserved among eukaryotes, suggesting evolutionary conservation of this interaction mode between SF3b49 RRM1 and SF3b145.
en_US
dc.language.iso
en
en_US
dc.publisher
Wiley
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject
nuclear magnetic resonance
en_US
dc.subject
RNA recognition motif
en_US
dc.subject
SF3b49
en_US
dc.subject
SF3b145
en_US
dc.subject
U2 snRNP
en_US
dc.title
Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
dc.date.published
2016-11-27
ethz.journal.title
Protein science
ethz.journal.volume
26
en_US
ethz.journal.issue
2
en_US
ethz.journal.abbreviated
Protein sci. (Print)
ethz.pages.start
280
en_US
ethz.pages.end
291
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.nebis
000627420
ethz.publication.place
Chichester
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02515 - Laboratorium für Physikalische Chemie / Laboratory of Physical Chemistry::03782 - Riek, Roland / Riek, Roland
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02515 - Laboratorium für Physikalische Chemie / Laboratory of Physical Chemistry::03782 - Riek, Roland / Riek, Roland
ethz.date.deposited
2017-06-12T18:07:23Z
ethz.source
ECIT
ethz.identifier.importid
imp5936551113d8d45947
ethz.ecitpid
pub:188099
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-18T14:57:54Z
ethz.rosetta.lastUpdated
2018-11-05T14:56:40Z
ethz.rosetta.versionExported
true
ethz.COinS
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