Network dynamics of the yeast methyltransferome
Authors:Guri Giaever1, Elena Lissina1 and Corey Nislow1
doi: 10.15698/mic2019.08.687
Volume 6, pp. 356 to 369, published 09/07/2019.
1 Department of Pharmaceutical Sciences, University of British Columbia, Vancouver, BC, Canada V6T 1Z3.
Keywords:
SAM methyltransferase, histone methyltransferase, genetic interaction, phospholipid, COMPASS.
Corresponding Author(s):
Conflict of interest statement:
The authors declare that they have no conflict of inter-ests.
Please cite this article as:
Guri Giaever, Elena Lissina and Corey Nislow (2019). Network dynamics of the yeast methyltransferome. Microbial Cell 6(8): 356-369. doi: 10.15698/mic2019.08.687
© 2019 Giaever et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduc-tion in any medium, provided the original author and source are acknowledged.
Abstract:
Sulfur assimilation and the biosynthesis of methionine, cysteine and S-adenosylmethionine (SAM) are critical to life. As a cofactor, SAM is required for the activity of most methyltransferases (MTases) and as such has broad impact on diverse cellular processes. Assigning function to MTases remains a challenge however, as many MTases are partially redundant, they often have multiple cellular roles and these activities can be condition-dependent. To address these challenges, we performed a systematic synthetic genetic analysis of all pairwise MTase double mutations in normal and stress conditions (16°C, 37°C, and LiCl) resulting in an unbiased comprehensive overview of the complexity and plasticity of the methyltransferome. Based on this network, we performed biochemical analysis of members of the histone H3K4 COMPASS complex and the phospholipid methyltransferase OPI3 to reveal a new role for a phospholipid methyltransferase in mediating histone methylation (H3K4) which underscores a potential link between lipid homeostasis and histone methylation. Our findings provide a valuable resource to study methyltransferase function, the dynamics of the methyltransferome, genetic crosstalk between biological processes and the dynamics of the methyltransferome in response to cellular stress.