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Evolution of a domain conserved in microtubule-associated proteins of eukaryotes
KTH, School of Biotechnology (BIO).
KTH, School of Computer Science and Communication (CSC).
KTH, School of Biotechnology (BIO).
KTH, School of Computer Science and Communication (CSC).
2008 (English)In: Advances and Applications in Bioinformatics and Chemistry, ISSN 1178-6949, Vol. 1, no 1, 51-69 p.Article in journal (Refereed) Published
Abstract [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.

Place, publisher, year, edition, pages
Dovepress , 2008. Vol. 1, no 1, 51-69 p.
Keyword [en]
TPX2 domain, MAP20, evolution, microtubule, cellulose, bioinformatics
National Category
Biochemistry and Molecular Biology
Research subject
SRA - Molecular Bioscience
Identifiers
URN: urn:nbn:se:kth:diva-39797DOI: 10.2147/AABC.S3211Scopus ID: 2-s2.0-58349099262OAI: oai:DiVA.org:kth-39797DiVA: diva2:440453
Note

QC 20111115

Available from: 2011-09-13 Created: 2011-09-13 Last updated: 2017-12-08Bibliographically approved

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Publisher's full textScopushttp://dx.doi.org/10.2147/AABC.S3211

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