| http://purl.uniprot.org/citations/7775576 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7775576 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7775576 | http://www.w3.org/2000/01/rdf-schema#comment | "In Tetrahymena, at least 17 distinct microtubule structures are assembled from a single primary sequence type of alpha- and beta-tubulin heterodimer, precluding distinctions among microtubular systems based on tubulin primary sequence isotypes. Tetrahymena tubulins also are modified by several types of posttranslational reactions including acetylation of alpha-tubulin at lysine 40, a modification found in most eukaryotes. In Tetrahymena, axonemal alpha-tubulin and numerous other microtubules are acetylated. We completely replaced the single type of alpha-tubulin gene in the macronucleus with a version encoding arginine instead of lysine 40 and therefore cannot be acetylated at this position. No acetylated tubulin was detectable in these transformants using a monoclonal antibody specific for acetylated lysine 40. Surprisingly, mutants lacking detectable acetylated tubulin are indistinguishable from wild-type cells. Thus, acetylation of alpha-tubulin at lysine 40 is non-essential in Tetrahymena. In addition, isoelectric focusing gel analysis of axonemal tubulin from cells unable to acetylate alpha-tubulin leads us to conclude that: (a) most or all ciliary alpha-tubulin is acetylated, (b) other lysines cannot be acetylated to compensate for loss of acetylation at lysine 40, and (c) acetylated alpha-tubulin molecules in wild-type cells contain one or more additional charge-altering modifications."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.129.5.1301"xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.129.5.1301"xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gu L."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gu L."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gaertig J."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gaertig J."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gorovsky M.A."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Gorovsky M.A."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Bowen J."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Bowen J."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Cruz M.A."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Cruz M.A."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Pennock D.G."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/author | "Pennock D.G."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/pages | "1301-1310"xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/pages | "1301-1310"xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/title | "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila."xsd:string |
| http://purl.uniprot.org/citations/7775576 | http://purl.uniprot.org/core/title | "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila."xsd:string |