A new class of microtubule-associated proteins in plants
In plants there are three microtubule arrays involved in cellular morphogenesis that have no equivalent in animal cells. In animals, microtubules are decorated by another class of proteins – the structural MAPS – which serve to stabilize microtubules and assist in their organization. The best-studie...
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| Veröffentlicht in: | Nature cell biology 2000-10, Vol.2 (10), p.750-753 |
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| creator | Smertenko, Andrei Saleh, Norihan Igarashi, Hisako Mori, Hitoshi Hauser-Hahn, Isolde Jiang, Chang-Jie Sonobe, Seiji Lloyd, Clive W. Hussey, Patrick J. |
| description | In plants there are three microtubule arrays involved in cellular morphogenesis that have no equivalent in animal cells. In animals, microtubules are decorated by another class of proteins – the structural MAPS – which serve to stabilize microtubules and assist in their organization. The best-studied members of this class in plants are the MAP-65 proteins that can be purified together with plant microtubules after several cycles of polymerization and depolymerization. Here we identify three similar MAP-65 complementary DNAs representing a small gene family named NtMAP65-1, which encode a new set of proteins, collectively called NtMAP65-1. We show that NtMAP65-1 protein localizes to areas of overlapping microtubules, indicating that it may function in the behaviour of antiparallel microtubules in the mitotic spindle and the cytokinetic phragmoplast. |
| doi_str_mv | 10.1038/35036390 |
| format | Article |
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In animals, microtubules are decorated by another class of proteins – the structural MAPS – which serve to stabilize microtubules and assist in their organization. The best-studied members of this class in plants are the MAP-65 proteins that can be purified together with plant microtubules after several cycles of polymerization and depolymerization. Here we identify three similar MAP-65 complementary DNAs representing a small gene family named NtMAP65-1, which encode a new set of proteins, collectively called NtMAP65-1. We show that NtMAP65-1 protein localizes to areas of overlapping microtubules, indicating that it may function in the behaviour of antiparallel microtubules in the mitotic spindle and the cytokinetic phragmoplast.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/35036390</identifier><identifier>PMID: 11025667</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Arrays ; Biomedical and Life Sciences ; brief-communication ; Cancer Research ; Cell Biology ; Cell Compartmentation ; Cell cycle ; Cloning ; Developmental Biology ; DNA, Complementary - genetics ; DNA, Plant - genetics ; Fluorescent Antibody Technique ; Life Sciences ; Methods ; Microtubule-Associated Proteins - isolation & purification ; Microtubules ; Molecular Sequence Data ; Morphogenesis ; Nicotiana - genetics ; Physiological aspects ; Plant proteins ; Plant Proteins - genetics ; Plant Proteins - isolation & purification ; Plants, Toxic ; Polymerization ; Protein microarrays ; Proteins ; Sequence Analysis ; Sequence Homology, Amino Acid ; Stains & staining ; Stem Cells ; Tobacco</subject><ispartof>Nature cell biology, 2000-10, Vol.2 (10), p.750-753</ispartof><rights>Macmillan Magazines Ltd. 2000</rights><rights>COPYRIGHT 2000 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Oct 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c507t-ccb974dca14a04a16086f992355e780dbc1656882fd41972e875d718ace147933</citedby><cites>FETCH-LOGICAL-c507t-ccb974dca14a04a16086f992355e780dbc1656882fd41972e875d718ace147933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/35036390$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/35036390$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11025667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smertenko, Andrei</creatorcontrib><creatorcontrib>Saleh, Norihan</creatorcontrib><creatorcontrib>Igarashi, Hisako</creatorcontrib><creatorcontrib>Mori, Hitoshi</creatorcontrib><creatorcontrib>Hauser-Hahn, Isolde</creatorcontrib><creatorcontrib>Jiang, Chang-Jie</creatorcontrib><creatorcontrib>Sonobe, Seiji</creatorcontrib><creatorcontrib>Lloyd, Clive W.</creatorcontrib><creatorcontrib>Hussey, Patrick J.</creatorcontrib><title>A new class of microtubule-associated proteins in plants</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>In plants there are three microtubule arrays involved in cellular morphogenesis that have no equivalent in animal cells. In animals, microtubules are decorated by another class of proteins – the structural MAPS – which serve to stabilize microtubules and assist in their organization. The best-studied members of this class in plants are the MAP-65 proteins that can be purified together with plant microtubules after several cycles of polymerization and depolymerization. Here we identify three similar MAP-65 complementary DNAs representing a small gene family named NtMAP65-1, which encode a new set of proteins, collectively called NtMAP65-1. We show that NtMAP65-1 protein localizes to areas of overlapping microtubules, indicating that it may function in the behaviour of antiparallel microtubules in the mitotic spindle and the cytokinetic phragmoplast.</description><subject>Amino Acid Sequence</subject><subject>Arrays</subject><subject>Biomedical and Life Sciences</subject><subject>brief-communication</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell Compartmentation</subject><subject>Cell cycle</subject><subject>Cloning</subject><subject>Developmental Biology</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Plant - genetics</subject><subject>Fluorescent Antibody Technique</subject><subject>Life Sciences</subject><subject>Methods</subject><subject>Microtubule-Associated Proteins - isolation & purification</subject><subject>Microtubules</subject><subject>Molecular Sequence Data</subject><subject>Morphogenesis</subject><subject>Nicotiana - genetics</subject><subject>Physiological aspects</subject><subject>Plant proteins</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plants, Toxic</subject><subject>Polymerization</subject><subject>Protein microarrays</subject><subject>Proteins</subject><subject>Sequence Analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Stains & staining</subject><subject>Stem 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| subjects | Amino Acid Sequence Arrays Biomedical and Life Sciences brief-communication Cancer Research Cell Biology Cell Compartmentation Cell cycle Cloning Developmental Biology DNA, Complementary - genetics DNA, Plant - genetics Fluorescent Antibody Technique Life Sciences Methods Microtubule-Associated Proteins - isolation & purification Microtubules Molecular Sequence Data Morphogenesis Nicotiana - genetics Physiological aspects Plant proteins Plant Proteins - genetics Plant Proteins - isolation & purification Plants, Toxic Polymerization Protein microarrays Proteins Sequence Analysis Sequence Homology, Amino Acid Stains & staining Stem Cells Tobacco |
| title | A new class of microtubule-associated proteins in plants |
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