New publication from the Bui Lab
Effect of 伪-tubulin acetylation on the doublet microtubule structure.
Acetylation of 伪-tubulin at the lysine 40 residue (伪K40) by 伪TAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that acetylated microtubules are more stable and damage resistant. 伪K40 acetylation is the only known microtubule luminal post-translational modification site. The luminal location suggests that the modification tunes the lateral interaction of protofilaments inside the microtubule. In this study, we examined the effect of tubulin acetylation on the doublet microtubule (DMT) in the cilia of聽Tetrahymena thermophila聽using a combination of cryo-electron microscopy, molecular dynamics, and mass spectrometry. We found that 伪K40 acetylation exerts a small-scale effect on the DMT structure and stability by influencing the lateral rotational angle. In addition, comparative mass spectrometry revealed a link between 伪K40 acetylation and phosphorylation in cilia.