Evolution of a domain conserved in microtubule-associated proteins of eukaryotes.
Identifieur interne : 003927 ( Main/Exploration ); précédent : 003926; suivant : 003928Evolution of a domain conserved in microtubule-associated proteins of eukaryotes.
Auteurs : Alex S. Rajangam [Suède] ; Hongqian Yang ; Tuula T. Teeri ; Lars ArvestadSource :
- Advances and applications in bioinformatics and chemistry : AABC [ 1178-6949 ] ; 2008.
Abstract
The microtubule network, the major organelle of the eukaryotic cytoskeleton, is involved in cell division and differentiation but also with many other cellular functions. In plants, microtubules seem to be involved in the ordered deposition of cellulose microfibrils by a so far unknown mechanism. Microtubule-associated proteins (MAP) typically contain various domains targeting or binding proteins with different functions to microtubules. Here we have investigated a proposed microtubule-targeting domain, TPX2, first identified in the Kinesin-like protein 2 in Xenopus. A TPX2 containing microtubule binding protein, PttMAP20, has been recently identified in poplar tissues undergoing xylogenesis. Furthermore, the herbicide 2,6-dichlorobenzonitrile (DCB), which is a known inhibitor of cellulose synthesis, was shown to bind specifically to PttMAP20. It is thus possible that PttMAP20 may have a role in coupling cellulose biosynthesis and the microtubular networks in poplar secondary cell walls. In order to get more insight into the occurrence, evolution and potential functions of TPX2-containing proteins we have carried out bioinformatic analysis for all genes so far found to encode TPX2 domains with special reference to poplar PttMAP20 and its putative orthologs in other plants.
DOI: 10.2147/aabc.s3211
PubMed: 21918606
PubMed Central: PMC3169935
Affiliations:
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Rajangam</name><affiliation wicri:level="3"><nlm:affiliation>KTH Biotechnology, Swedish Center for Biomimetic Fiber Engineering, AlbaNova, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>KTH Biotechnology, Swedish Center for Biomimetic Fiber Engineering, AlbaNova, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Yang, Hongqian" sort="Yang, Hongqian" uniqKey="Yang H" first="Hongqian" last="Yang">Hongqian Yang</name></author><author><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></author><author><name sortKey="Arvestad, Lars" sort="Arvestad, Lars" uniqKey="Arvestad L" first="Lars" last="Arvestad">Lars Arvestad</name></author></analytic><series><title level="j">Advances and applications in bioinformatics and chemistry : AABC</title><idno type="ISSN">1178-6949</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The microtubule network, the major organelle of the eukaryotic cytoskeleton, is involved in cell division and differentiation but also with many other cellular functions. In plants, microtubules seem to be involved in the ordered deposition of cellulose microfibrils by a so far unknown mechanism. Microtubule-associated proteins (MAP) typically contain various domains targeting or binding proteins with different functions to microtubules. Here we have investigated a proposed microtubule-targeting domain, TPX2, first identified in the Kinesin-like protein 2 in Xenopus. A TPX2 containing microtubule binding protein, PttMAP20, has been recently identified in poplar tissues undergoing xylogenesis. Furthermore, the herbicide 2,6-dichlorobenzonitrile (DCB), which is a known inhibitor of cellulose synthesis, was shown to bind specifically to PttMAP20. It is thus possible that PttMAP20 may have a role in coupling cellulose biosynthesis and the microtubular networks in poplar secondary cell walls. In order to get more insight into the occurrence, evolution and potential functions of TPX2-containing proteins we have carried out bioinformatic analysis for all genes so far found to encode TPX2 domains with special reference to poplar PttMAP20 and its putative orthologs in other plants.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">21918606</PMID><DateCompleted><Year>2011</Year><Month>11</Month><Day>10</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1178-6949</ISSN><JournalIssue CitedMedium="Print"><Volume>1</Volume><PubDate><Year>2008</Year></PubDate></JournalIssue><Title>Advances and applications in bioinformatics and chemistry : AABC</Title><ISOAbbreviation>Adv Appl Bioinform Chem</ISOAbbreviation></Journal><ArticleTitle>Evolution of a domain conserved in microtubule-associated proteins of eukaryotes.</ArticleTitle><Pagination><MedlinePgn>51-69</MedlinePgn></Pagination><Abstract><AbstractText>The microtubule network, the major organelle of the eukaryotic cytoskeleton, is involved in cell division and differentiation but also with many other cellular functions. In plants, microtubules seem to be involved in the ordered deposition of cellulose microfibrils by a so far unknown mechanism. Microtubule-associated proteins (MAP) typically contain various domains targeting or binding proteins with different functions to microtubules. Here we have investigated a proposed microtubule-targeting domain, TPX2, first identified in the Kinesin-like protein 2 in Xenopus. A TPX2 containing microtubule binding protein, PttMAP20, has been recently identified in poplar tissues undergoing xylogenesis. Furthermore, the herbicide 2,6-dichlorobenzonitrile (DCB), which is a known inhibitor of cellulose synthesis, was shown to bind specifically to PttMAP20. It is thus possible that PttMAP20 may have a role in coupling cellulose biosynthesis and the microtubular networks in poplar secondary cell walls. In order to get more insight into the occurrence, evolution and potential functions of TPX2-containing proteins we have carried out bioinformatic analysis for all genes so far found to encode TPX2 domains with special reference to poplar PttMAP20 and its putative orthologs in other plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rajangam</LastName><ForeName>Alex S</ForeName><Initials>AS</Initials><AffiliationInfo><Affiliation>KTH Biotechnology, Swedish Center for Biomimetic Fiber Engineering, AlbaNova, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Hongqian</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</Initials></Author><Author ValidYN="Y"><LastName>Arvestad</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType 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Teeri</name><name sortKey="Yang, Hongqian" sort="Yang, Hongqian" uniqKey="Yang H" first="Hongqian" last="Yang">Hongqian Yang</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Rajangam, Alex S" sort="Rajangam, Alex S" uniqKey="Rajangam A" first="Alex S" last="Rajangam">Alex S. Rajangam</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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