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S-Adenosylmethionine Synthetase Is Required for Cell Growth, Maintenance of G0 Phase, and Termination of Quiescence in Fission Yeast

S-adenosylmethionine is an important compound, because it serves as the methyl donor in most methyl transfer reactions, including methylation of proteins, nucleic acids, and lipids. However, cellular defects in the genetic disruption of S-adenosylmethionine synthesis are not well understood. Here, w...

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Published in:iScience 2018-07, Vol.5, p.38-51
Main Authors: Hayashi, Takeshi, Teruya, Takayuki, Chaleckis, Romanas, Morigasaki, Susumu, Yanagida, Mitsuhiro
Format: Article
Language:English
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Summary:S-adenosylmethionine is an important compound, because it serves as the methyl donor in most methyl transfer reactions, including methylation of proteins, nucleic acids, and lipids. However, cellular defects in the genetic disruption of S-adenosylmethionine synthesis are not well understood. Here, we report the isolation and characterization of temperature-sensitive mutants of fission yeast S-adenosylmethionine synthetase (Sam1). Levels of S-adenosylmethionine and methylated histone H3 were greatly diminished in sam1 mutants. sam1 mutants stopped proliferating in vegetative culture and arrested specifically in G2 phase without cell elongation. Furthermore, sam1 mutants lost viability during nitrogen starvation-induced G0 phase quiescence. After release from the G0 state, sam1 mutants could neither increase in cell size nor re-initiate DNA replication in the rich medium. Sam1 is thus required for cell growth and proliferation, and maintenance of and exit from quiescence. sam1 mutants lead to broad cellular and drug response defects, as expected, since S. pombe contains more than 90 S-adenosylmethionine-dependent methyltransferases. [Display omitted] •Fission yeast temperature-sensitive mutant strains of SAM synthetase were isolated•SAM synthetase is essential for both proliferation and quiescence•SAM synthetase mutants show pleiotropic drug sensitivities•Extensive changes occur in the metabolic profiles of SAM synthetase mutants Molecular Mechanism of Behavior; Cell Biology; Functional Aspects of Cell Biology; Model Organism
ISSN:2589-0042
2589-0042
DOI:10.1016/j.isci.2018.06.011