Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila.

• DOI: 10.1083/jcb.129.5.1301
• Publication Date: 2004-05-15T01:23:47Z
• Authors: J Gaertig; M A Cruz; J Bowen; L Gu; D G Pennock; M A Gorovsky
• Keywords: Macronucleus

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 isotypes. Tetrahymena tubulins also modified by several types posttranslational reactions including acetylation alpha-tubulin lysine 40, modification found in most eukaryotes. axonemal numerous other microtubules acetylated. We completely replaced the gene macronucleus with version encoding arginine instead 40 therefore cannot be acetylated this position. No was detectable these transformants using monoclonal antibody specific for 40. Surprisingly, mutants lacking indistinguishable wild-type cells. Thus, is non-essential Tetrahymena. addition, isoelectric focusing gel analysis cells unable to acetylate leads us conclude that: (a) or all ciliary acetylated, (b) lysines compensate loss (c) molecules contain one more additional charge-altering modifications.