| http://purl.uniprot.org/citations/17394772 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17394772 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17394772 | http://www.w3.org/2000/01/rdf-schema#comment | "In Arabidopsis thaliana, the microtubule-associated protein AtMAP65-1 shows various functions on microtubule dynamics and organizations. However, it is still an open question about whether AtMAP65-1 binds to tubulin dimers and how it regulates microtubule dynamics. In present study, the tubulin-binding activity of AtMAP65-1 was investigated. Pull-down and co-sedimentation experiments demonstrated that AtMAP65-1 bound to tubulin dimers, at a molar ratio of 1 : 1. Cross-linking experiments showed that AtMAP65-1 bound to tubulin dimers by interacting with alpha-tubulin of the tubulin heterodimer. Interfering the bundling effect of AtMAP65-1 by addition of salt and monitoring the tubulin assembly, the experiment results indicated that AtMAP65-1 promoted tubulin assembly by interacting with tubulin dimers. In addition, five truncated versions of AtMAP65-1, namely AtMAP65-1 deltaN339 (amino acids 340-587); AtMAP65-1 deltaN494 (amino acids 495-587); AtMAP65-1 340-494 (amino acids 340-494); AtMAP65-1 deltaC495 (amino acids 1-494) and AtMAP65-1 deltaC340 (amino acids 1-339), were tested for their binding activities and roles in tubulin polymerization in vitro. Four (AtMAP65-1 deltaN339, deltaN494, AtMAP65-1 340-494 and deltaC495) from the five truncated proteins were able to co-sediment with microtubules, and three (AtMAP65-1 deltaN339, deltaN494 and AtMAP65-1 340-494) of them could bind to tubulin dimers in vitro. Among the three truncated proteins, AtMAP65-1 deltaN339 showed the greatest activity to promote tubulin polymerization, AtMAP65-1 deltaN494 exhibited almost the same activity as the full length protein in promoting tubulin assembly, and AtMAP65-1 340-494 had minor activity to promote tubulin assembly. On the contrast, AtMAP65-1 deltaC495, which bound to microtubules but not to tubulin dimers, did not affect tubulin assembly. Our study suggested that AtMAP65-1 might promote tubulin assembly by binding to tubulin dimers in vivo."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.org/dc/terms/identifier | "doi:10.5483/bmbrep.2007.40.2.218"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.org/dc/terms/identifier | "doi:10.5483/bmbrep.2007.40.2.218"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Li H."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Yuan M."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Yuan M."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Mao T."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/author | "Mao T."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/name | "J. Biochem. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/name | "J. Biochem. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/pages | "218-225"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/pages | "218-225"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/title | "AtMAP65-1 binds to tubulin dimers to promote tubulin assembly."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/title | "AtMAP65-1 binds to tubulin dimers to promote tubulin assembly."xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/volume | "40"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://purl.uniprot.org/core/volume | "40"xsd:string |
| http://purl.uniprot.org/citations/17394772 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17394772 |
| http://purl.uniprot.org/citations/17394772 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17394772 |
| http://purl.uniprot.org/citations/17394772 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17394772 |
| http://purl.uniprot.org/citations/17394772 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17394772 |