Disease relevance of SAM1

• The rat liver S-adenosylmethionine synthetase also shows 52% similarity with the deduced amino acid sequence of the MetK gene encoding the S-adenosylmethionine synthetase in Escherichia coli [1].
• We have isolated cDNA clones encoding the rat liver S-adenosylmethionine synthetase by means of immunological screening from a phage lambda gt 11 expression library containing cDNA synthesized from adult rat liver poly(A)-RNA [1].

High impact information on SAM1

• The rate of ectopic recombination between two unlinked, homologous loci, SAM1 and SAM2, is sixfold higher in cells containing a top3 null mutation than in wild-type cells [2].
• The results show that the expression of the two SAM genes is regulated differently, SAM2 being induced by the presence of excess methionine in the growth medium and SAM1 being repressed under the same conditions [3].
• SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression [4].
• The DNA sequence of SAM1 is reported [4].
• Intense biochemical and genetic research on the eth-1r mutant of Neurospora crassa suggested that this locus might encode S-adenosylmethionine synthetase (S-Adomet synthetase) [5].

Biological context of SAM1

• Single frameshift mutations were introduced into the 5' end of SAM1 and the 3' end of SAM2 by restriction site ablation [6].
• SAM1 and SAM2, located on chromosomes XII and IV, respectively, encode functionally equivalent although differentially regulated AdoMet synthetases [6].
• Null mutations in three recombination and DNA repair genes were studied to determine their effects on mitotic recombination between the duplicate AdoMet (S-adenosylmethionine) synthetase genes (SAM1 and SAM2) in Saccharomyces cerevisiae [6].
• A study of in vivo and in vitro methylation of tRNAs in regulatory mutants affected in methionine-mediated repression (eth2, eth3, eth10) has led to the following results: 1) The eth2-2 carrying strain presents a great undermethylation of its tRNAs of the same order of magnitude as observed during methionine starvation of methionine auxotrophs [7].
• In haploid strains, gene sam1 is essential for growth; if weakly expressed, cells mate and sporulate at a reduced rate [8].

Anatomical context of SAM1

• Polyclonal anti-human lymphocyte AdoMet synthetase crossreacted with enzyme from rat liver (beta isozyme), Escherichia coli and yeast [9].

Associations of SAM1 with chemical compounds

• SAM1 and SAM3 mRNAs accumulated in the root in response to NaCl, mannitol or ABA treatments [10].
• The inhibition of S-adenosylmethionine synthetase by trifluoromethionine prevents both germination and protein synthesis [11].
• By flow cytometric analysis, a monoclonal antibody (MAb) directed against human alpha 5 integrin subunit (clone SAM-1) and two different antisera to FNr positively stained C. tropicalis, C. stellatoidea and C. glabrata, with the greatest expression observed for C. tropicalis [12].

Other interactions of SAM1

• The deduced amino acid sequence of rat liver S-adenosylmethionine synthetase was 68% similar to those of yeast S-adenosylmethionine synthetases encoded by two unlinked genes SAM1 and SAM2 [1].
• Ymr116c was PKA-independent, while Pgi1p, Sam1p, Gdh1p and Vma1p were fully PKA-dependent [13].

Analytical, diagnostic and therapeutic context of SAM1

• eth-1, the Neurospora crassa locus encoding S-adenosylmethionine synthetase: molecular cloning, sequence analysis and in vivo overexpression [5].

References