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Conserved SAMS function in regulating egg-laying in C. elegans.
MedLine Citation:
PMID:  23316847     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Hiroko Tamiya; Keiko Hirota; Yuta Takahashi; Hiroaki Daitoku; Yuta Kaneko; Genki Sakuta; Kei Iizuka; Satoshi Watanabe; Naoaki Ishii; Akiyoshi Fukamizu
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-15
Journal Detail:
Title:  Journal of receptor and signal transduction research     Volume:  -     ISSN:  1532-4281     ISO Abbreviation:  J. Recept. Signal Transduct. Res.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9509432     Medline TA:  J Recept Signal Transduct Res     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Life Science Center, Tsukuba Advanced Research Alliance, Graduate School of Life and Environmental Sciences, University of Tsukuba , 1-1-1 Tennoudai, Tsukuba, Ibaraki , Japan , and.
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