Myosin diversity in the diatom Phaeodactylum tricornutum.
Identifieur interne : 001876 ( Main/Exploration ); précédent : 001875; suivant : 001877Myosin diversity in the diatom Phaeodactylum tricornutum.
Auteurs : Matthew B. Heintzelman [États-Unis] ; Matthew E. EnriquezSource :
- Cytoskeleton (Hoboken, N.J.) [ 1949-3592 ] ; 2010.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Clonage moléculaire (MeSH), Diatomées (génétique), Diatomées (métabolisme), Données de séquences moléculaires (MeSH), Motifs d'acides aminés (génétique), Myosines (génétique), Phylogenèse (MeSH), Structure tertiaire des protéines (génétique), Séquence consensus (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Myosins.
- genetics : Amino Acid Motifs, Diatoms, Protein Structure, Tertiary.
- metabolism : Diatoms.
- Amino Acid Sequence, Cloning, Molecular, Consensus Sequence, Molecular Sequence Data, Phylogeny, Sequence Alignment.
Abstract
This report describes the domain architecture of ten myosins cloned from the pennate diatom Phaeodactylum tricornutum. Several of the P. tricornutum myosins show similarity to myosins from the centric diatom Thalassiosira pseudonana as well as to one myosin from the oomycete Phytophthora ramorum. The P. tricornutum myosins, ranging in size from 126 kDa to over 250 kDa, all possess the canonical head, neck and tail domains common to most myosins, though variations in each of these domains is evident. Among the features distinguishing several of the diatom myosin head domains are N-terminal SH3-like domains, variations in or near the P-loop and Loop 1 regions close to the nucleotide binding pocket, and extended converter domains. Variations in the length of the neck domain or lever arm, defined by the light chain-binding IQ motifs, are apparent with the different diatom myosins predicted to contain from one to nine IQ motifs. Protein domains found within the P. tricornutum myosin tails include regions of coiled-coil structure, ankyrin repeats, CBS domain pairs, a PB1 domain, a kinase domain and a FYVE-finger motif. As many of these features have never before been characterized in myosins of any type, it is likely that these new diatom myosins will expand the repertoire of known myosin behaviors.
DOI: 10.1002/cm.20431
PubMed: 20217677
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Myosin diversity in the diatom Phaeodactylum tricornutum.</title>
<author><name sortKey="Heintzelman, Matthew B" sort="Heintzelman, Matthew B" uniqKey="Heintzelman M" first="Matthew B" last="Heintzelman">Matthew B. Heintzelman</name>
<affiliation wicri:level="2"><nlm:affiliation>Program in Cell Biology and Biochemistry, Department of Biology, Bucknell University, Lewisburg, PA 17837, USA. mheintze@bucknell.edu</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Program in Cell Biology and Biochemistry, Department of Biology, Bucknell University, Lewisburg, PA 17837</wicri:regionArea>
<placeName><region type="state">Pennsylvanie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Enriquez, Matthew E" sort="Enriquez, Matthew E" uniqKey="Enriquez M" first="Matthew E" last="Enriquez">Matthew E. Enriquez</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2010">2010</date>
<idno type="RBID">pubmed:20217677</idno>
<idno type="pmid">20217677</idno>
<idno type="doi">10.1002/cm.20431</idno>
<idno type="wicri:Area/Main/Corpus">001939</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001939</idno>
<idno type="wicri:Area/Main/Curation">001939</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001939</idno>
<idno type="wicri:Area/Main/Exploration">001939</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Myosin diversity in the diatom Phaeodactylum tricornutum.</title>
<author><name sortKey="Heintzelman, Matthew B" sort="Heintzelman, Matthew B" uniqKey="Heintzelman M" first="Matthew B" last="Heintzelman">Matthew B. Heintzelman</name>
<affiliation wicri:level="2"><nlm:affiliation>Program in Cell Biology and Biochemistry, Department of Biology, Bucknell University, Lewisburg, PA 17837, USA. mheintze@bucknell.edu</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Program in Cell Biology and Biochemistry, Department of Biology, Bucknell University, Lewisburg, PA 17837</wicri:regionArea>
<placeName><region type="state">Pennsylvanie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Enriquez, Matthew E" sort="Enriquez, Matthew E" uniqKey="Enriquez M" first="Matthew E" last="Enriquez">Matthew E. Enriquez</name>
</author>
</analytic>
<series><title level="j">Cytoskeleton (Hoboken, N.J.)</title>
<idno type="eISSN">1949-3592</idno>
<imprint><date when="2010" type="published">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (genetics)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Consensus Sequence (MeSH)</term>
<term>Diatoms (genetics)</term>
<term>Diatoms (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Myosins (genetics)</term>
<term>Phylogeny (MeSH)</term>
<term>Protein Structure, Tertiary (genetics)</term>
<term>Sequence Alignment (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Diatomées (génétique)</term>
<term>Diatomées (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Motifs d'acides aminés (génétique)</term>
<term>Myosines (génétique)</term>
<term>Phylogenèse (MeSH)</term>
<term>Structure tertiaire des protéines (génétique)</term>
<term>Séquence consensus (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Myosins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Diatoms</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Diatomées</term>
<term>Motifs d'acides aminés</term>
<term>Myosines</term>
<term>Structure tertiaire des protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Diatoms</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Diatomées</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Cloning, Molecular</term>
<term>Consensus Sequence</term>
<term>Molecular Sequence Data</term>
<term>Phylogeny</term>
<term>Sequence Alignment</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Phylogenèse</term>
<term>Séquence consensus</term>
<term>Séquence d'acides aminés</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">This report describes the domain architecture of ten myosins cloned from the pennate diatom Phaeodactylum tricornutum. Several of the P. tricornutum myosins show similarity to myosins from the centric diatom Thalassiosira pseudonana as well as to one myosin from the oomycete Phytophthora ramorum. The P. tricornutum myosins, ranging in size from 126 kDa to over 250 kDa, all possess the canonical head, neck and tail domains common to most myosins, though variations in each of these domains is evident. Among the features distinguishing several of the diatom myosin head domains are N-terminal SH3-like domains, variations in or near the P-loop and Loop 1 regions close to the nucleotide binding pocket, and extended converter domains. Variations in the length of the neck domain or lever arm, defined by the light chain-binding IQ motifs, are apparent with the different diatom myosins predicted to contain from one to nine IQ motifs. Protein domains found within the P. tricornutum myosin tails include regions of coiled-coil structure, ankyrin repeats, CBS domain pairs, a PB1 domain, a kinase domain and a FYVE-finger motif. As many of these features have never before been characterized in myosins of any type, it is likely that these new diatom myosins will expand the repertoire of known myosin behaviors.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20217677</PMID>
<DateCompleted><Year>2010</Year>
<Month>09</Month>
<Day>30</Day>
</DateCompleted>
<DateRevised><Year>2014</Year>
<Month>07</Month>
<Day>24</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1949-3592</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>67</Volume>
<Issue>3</Issue>
<PubDate><Year>2010</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>Cytoskeleton (Hoboken, N.J.)</Title>
<ISOAbbreviation>Cytoskeleton (Hoboken)</ISOAbbreviation>
</Journal>
<ArticleTitle>Myosin diversity in the diatom Phaeodactylum tricornutum.</ArticleTitle>
<Pagination><MedlinePgn>142-51</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1002/cm.20431</ELocationID>
<Abstract><AbstractText>This report describes the domain architecture of ten myosins cloned from the pennate diatom Phaeodactylum tricornutum. Several of the P. tricornutum myosins show similarity to myosins from the centric diatom Thalassiosira pseudonana as well as to one myosin from the oomycete Phytophthora ramorum. The P. tricornutum myosins, ranging in size from 126 kDa to over 250 kDa, all possess the canonical head, neck and tail domains common to most myosins, though variations in each of these domains is evident. Among the features distinguishing several of the diatom myosin head domains are N-terminal SH3-like domains, variations in or near the P-loop and Loop 1 regions close to the nucleotide binding pocket, and extended converter domains. Variations in the length of the neck domain or lever arm, defined by the light chain-binding IQ motifs, are apparent with the different diatom myosins predicted to contain from one to nine IQ motifs. Protein domains found within the P. tricornutum myosin tails include regions of coiled-coil structure, ankyrin repeats, CBS domain pairs, a PB1 domain, a kinase domain and a FYVE-finger motif. As many of these features have never before been characterized in myosins of any type, it is likely that these new diatom myosins will expand the repertoire of known myosin behaviors.</AbstractText>
<CopyrightInformation>(c) 2010 Wiley-Liss, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Heintzelman</LastName>
<ForeName>Matthew B</ForeName>
<Initials>MB</Initials>
<AffiliationInfo><Affiliation>Program in Cell Biology and Biochemistry, Department of Biology, Bucknell University, Lewisburg, PA 17837, USA. mheintze@bucknell.edu</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Enriquez</LastName>
<ForeName>Matthew E</ForeName>
<Initials>ME</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName>
<AccessionNumberList><AccessionNumber>GQ141540</AccessionNumber>
<AccessionNumber>GQ141541</AccessionNumber>
<AccessionNumber>GQ141542</AccessionNumber>
<AccessionNumber>GQ141543</AccessionNumber>
<AccessionNumber>GQ141544</AccessionNumber>
<AccessionNumber>GQ141545</AccessionNumber>
<AccessionNumber>GQ141546</AccessionNumber>
<AccessionNumber>GQ141547</AccessionNumber>
<AccessionNumber>GQ141548</AccessionNumber>
<AccessionNumber>GQ141549</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cytoskeleton (Hoboken)</MedlineTA>
<NlmUniqueID>101523844</NlmUniqueID>
<ISSNLinking>1949-3592</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>EC 3.6.4.1</RegistryNumber>
<NameOfSubstance UI="D009218">Myosins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016384" MajorTopicYN="N">Consensus Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017377" MajorTopicYN="N">Diatoms</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009218" MajorTopicYN="N">Myosins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year>
<Month>3</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>3</Month>
<Day>11</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>10</Month>
<Day>1</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">20217677</ArticleId>
<ArticleId IdType="doi">10.1002/cm.20431</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Pennsylvanie</li>
</region>
</list>
<tree><noCountry><name sortKey="Enriquez, Matthew E" sort="Enriquez, Matthew E" uniqKey="Enriquez M" first="Matthew E" last="Enriquez">Matthew E. Enriquez</name>
</noCountry>
<country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Heintzelman, Matthew B" sort="Heintzelman, Matthew B" uniqKey="Heintzelman M" first="Matthew B" last="Heintzelman">Matthew B. Heintzelman</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhytophthoraV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001876 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001876 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= PhytophthoraV1 |flux= Main |étape= Exploration |type= RBID |clé= pubmed:20217677 |texte= Myosin diversity in the diatom Phaeodactylum tricornutum. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:20217677" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \ | NlmPubMed2Wicri -a PhytophthoraV1
This area was generated with Dilib version V0.6.38. |