Ab initio detection of fuzzy amino acid tandem repeats in protein sequences
Identifieur interne : 000327 ( Pmc/Curation ); précédent : 000326; suivant : 000328Ab initio detection of fuzzy amino acid tandem repeats in protein sequences
Auteurs : Marco Pellegrini [Italie] ; Maria Elena Renda [Italie] ; Alessio Vecchio [Italie]Source :
- BMC Bioinformatics [ 1471-2105 ] ; 2012.
Abstract
Tandem repetitions within protein amino acid sequences often correspond to regular secondary structures and form multi-repeat 3D assemblies of varied size and function. Developing internal repetitions is one of the evolutionary mechanisms that proteins employ to adapt their structure and function under evolutionary pressure. While there is keen interest in understanding such phenomena, detection of repeating structures based only on sequence analysis is considered an arduous task, since structure and function is often preserved even under considerable sequence divergence (
In this paper we present
Url:
DOI: 10.1186/1471-2105-13-S3-S8
PubMed: 22536906
PubMed Central: 3402919
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Ab initio detection of fuzzy amino acid tandem repeats in protein sequences</title>
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<author><name sortKey="Renda, Maria Elena" sort="Renda, Maria Elena" uniqKey="Renda M" first="Maria Elena" last="Renda">Maria Elena Renda</name>
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<author><name sortKey="Vecchio, Alessio" sort="Vecchio, Alessio" uniqKey="Vecchio A" first="Alessio" last="Vecchio">Alessio Vecchio</name>
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<series><title level="j">BMC Bioinformatics</title>
<idno type="eISSN">1471-2105</idno>
<imprint><date when="2012">2012</date>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Tandem repetitions within protein amino acid sequences often correspond to regular secondary structures and form multi-repeat 3D assemblies of varied size and function. Developing internal repetitions is one of the evolutionary mechanisms that proteins employ to adapt their structure and function under evolutionary pressure. While there is keen interest in understanding such phenomena, detection of repeating structures based only on sequence analysis is considered an arduous task, since structure and function is often preserved even under considerable sequence divergence (<italic>fuzzy tandem repeats</italic>
).</p>
</sec>
<sec><title>Results</title>
<p>In this paper we present <italic>PTRStalker</italic>
, a new algorithm for <italic>ab-initio </italic>
detection of <italic>fuzzy tandem repeats </italic>
in protein amino acid sequences. In the reported results we show that by feeding <italic>PTRStalker </italic>
with amino acid sequences from the UniProtKB/Swiss-Prot database we detect novel tandemly repeated structures not captured by other state-of-the-art tools. Experiments with membrane proteins indicate that <italic>PTRStalker </italic>
can detect global symmetries in the primary structure which are then reflected in the tertiary structure.</p>
</sec>
<sec><title>Conclusions</title>
<p><italic>PTRStalker </italic>
is able to detect fuzzy tandem repeating structures in protein sequences, with performance beyond the current state-of-the art. Such a tool may be a valuable support to investigating protein structural properties when tertiary X-ray data is not available.</p>
</sec>
</div>
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<pmc article-type="research-article" xml:lang="en"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">BMC Bioinformatics</journal-id>
<journal-id journal-id-type="iso-abbrev">BMC Bioinformatics</journal-id>
<journal-title-group><journal-title>BMC Bioinformatics</journal-title>
</journal-title-group>
<issn pub-type="epub">1471-2105</issn>
<publisher><publisher-name>BioMed Central</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">22536906</article-id>
<article-id pub-id-type="pmc">3402919</article-id>
<article-id pub-id-type="publisher-id">1471-2105-13-S3-S8</article-id>
<article-id pub-id-type="doi">10.1186/1471-2105-13-S3-S8</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Proceedings</subject>
</subj-group>
</article-categories>
<title-group><article-title>Ab initio detection of fuzzy amino acid tandem repeats in protein sequences</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" corresp="yes" id="A1"><name><surname>Pellegrini</surname>
<given-names>Marco</given-names>
</name>
<xref ref-type="aff" rid="I1">1</xref>
<email>marco.pellegrini@iit.cnr.it</email>
</contrib>
<contrib contrib-type="author" id="A2"><name><surname>Renda</surname>
<given-names>Maria Elena</given-names>
</name>
<xref ref-type="aff" rid="I1">1</xref>
<email>elena.renda@iit.cnr.it</email>
</contrib>
<contrib contrib-type="author" id="A3"><name><surname>Vecchio</surname>
<given-names>Alessio</given-names>
</name>
<xref ref-type="aff" rid="I2">2</xref>
<email>a.vecchio@ing.unipi.it</email>
</contrib>
</contrib-group>
<aff id="I1"><label>1</label>
Istituto di Informatica e Telematica, CNR - Consiglio Nazionale delle Ricerche, Pisa I-56124, Italy</aff>
<aff id="I2"><label>2</label>
Dipartimento di Ingegneria dell'Informazione, Università di Pisa, Pisa I-56122, Italy</aff>
<pub-date pub-type="collection"><year>2012</year>
</pub-date>
<pub-date pub-type="epub"><day>21</day>
<month>3</month>
<year>2012</year>
</pub-date>
<volume>13</volume>
<issue>Suppl 3</issue>
<supplement><named-content content-type="supplement-title">ACM Conference on Bioinformatics, Computational Biology and Biomedicine 2011</named-content>
<named-content content-type="supplement-editor">Sun Kim and Wei Wang</named-content>
<named-content content-type="supplement-sponsor">Publication of this supplement has been supported by NSF support number NSF IIS1137427: III: Small: Women in Bioinformatics Initiative at ACM-BCB 2011.</named-content>
</supplement>
<fpage>S8</fpage>
<lpage>S8</lpage>
<permissions><copyright-statement>Copyright ©2012 Pellegrini et al.; licensee BioMed Central Ltd.</copyright-statement>
<copyright-year>2012</copyright-year>
<copyright-holder>Pellegrini et al.; licensee BioMed Central Ltd.</copyright-holder>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.0"><license-p>This is an open access article distributed under the terms of the Creative Commons Attribution License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/2.0">http://creativecommons.org/licenses/by/2.0</ext-link>
), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p>
</license>
</permissions>
<self-uri xlink:href="http://www.biomedcentral.com/1471-2105/13/S3/S8"></self-uri>
<abstract><sec><title>Background</title>
<p>Tandem repetitions within protein amino acid sequences often correspond to regular secondary structures and form multi-repeat 3D assemblies of varied size and function. Developing internal repetitions is one of the evolutionary mechanisms that proteins employ to adapt their structure and function under evolutionary pressure. While there is keen interest in understanding such phenomena, detection of repeating structures based only on sequence analysis is considered an arduous task, since structure and function is often preserved even under considerable sequence divergence (<italic>fuzzy tandem repeats</italic>
).</p>
</sec>
<sec><title>Results</title>
<p>In this paper we present <italic>PTRStalker</italic>
, a new algorithm for <italic>ab-initio </italic>
detection of <italic>fuzzy tandem repeats </italic>
in protein amino acid sequences. In the reported results we show that by feeding <italic>PTRStalker </italic>
with amino acid sequences from the UniProtKB/Swiss-Prot database we detect novel tandemly repeated structures not captured by other state-of-the-art tools. Experiments with membrane proteins indicate that <italic>PTRStalker </italic>
can detect global symmetries in the primary structure which are then reflected in the tertiary structure.</p>
</sec>
<sec><title>Conclusions</title>
<p><italic>PTRStalker </italic>
is able to detect fuzzy tandem repeating structures in protein sequences, with performance beyond the current state-of-the art. Such a tool may be a valuable support to investigating protein structural properties when tertiary X-ray data is not available.</p>
</sec>
</abstract>
<conference><conf-date>1-3 August 2011</conf-date>
<conf-name>ACM Conference on Bioinformatics, Computational Biology and Biomedicine 2011 (ACM-BCB)</conf-name>
<conf-loc>Chicago, IL, USA</conf-loc>
</conference>
</article-meta>
</front>
</pmc>
</record>
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