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Mass spectrometry of axonemes from Tetrahymena thermophila CU428 and acetylation mutants

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Apr 12, 2024 version files 1.82 GB

Abstract

Acetylation of α-tubulin at the lysine 40 residue (αK40) by the ATAT1/MEC-17 acetyltransferase influences the properties of microtubules and is a widespread phenomenon in eukaryotic cells. Previous research indicates that microtubules that undergo acetylation at αK40 are more stable and resilient to damage. Notably, αK40 acetylation represents the sole identified post-translational modification site within the microtubule lumen, suggesting its role in regulating the lateral interactions among protofilaments within the microtubule structure. This investigation focuses on evaluating the impact of tubulin acetylation on doublet microtubules present in the cilia of Tetrahymena thermophila, employing mass spectrometry analysis. Cilia samples derived from Tetrahymena wild type, acetylation mutants (K40R and MEC17-Knockout), and non-acetylation mutants (RIB72B-Knockout and RIB72AB-Knockout) underwent comparative mass spectrometry analysis. The results from mass spectrometry revealed a correlation between αK40 acetylation and phosphorylation within the ciliary structures.