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Conserved SAMS function in regulating egg-laying in C. elegans

Conserved SAMS function in regulating egg-laying in C. elegans

, , , , , , , , & show all
Pages 56-62 | Received 02 Nov 2012, Accepted 05 Dec 2012, Published online: 15 Jan 2013
 

Abstract

S-adenosyl-L-methionine (SAM) is an intermediate metabolite of methionine and serves as the methyl donor for many biological methylation reactions. The synthesis of SAM is catalyzed by SAM synthetase (SAMS), which transfers the adenosyl moiety of adenosine-5′-triphosphate to methionine. In the nematode Caenorhabditis elegans, four sams family genes, sams-1, -3, -4 and -5, are predicted to encode SAMS proteins. However, their physiological roles remain unclear. Here we show that the four predicted SAMS proteins in fact have the ability to catalyze the formation of SAM in vitro, and revealed that only sams-1 mutant animals among the family genes exhibited a significant reduction in egg-laying. Using transgenic animals carrying a transcriptional reporter for each sams gene promoter, we observed that each sams promoter confers a distinct expression pattern with respect to tissue, time of expression and expression level (i.e. promoter specificity). Promoter-swap experiments revealed that the ectopic expression of SAMS-3, -4 or -5 driven by the sams-1 promoter completely rescued egg-laying in sams-1 mutants. These data indicate that SAMS protein function is conserved throughout the entire family.

Acknowledgements

We thank Dr Shohei Mitani for generating C. elegans sams-3(tm4237) and sams-4(tm4235) strains. We thank Dr H. Robert Horvitz and Dr. Ryusuke Niwa for marker plasmids, Dr Andrew Fire for GFP expression vectors and members of the Fukamizu lab for helpful discussion. We also thank the Caenorhabditis Genetics Center and Japanese National Bioresource Project for the C. elegans strains.

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