High impact information on mtl-2

• Cu did not induce MT1 or MT2 mRNAs [1].
• After 10 mM Cd treatment, induction of MT1 and MT2 mRNA was three- and twofold higher, respectively, in daf-2 mutant worms than in wild-type [1].
• Likewise, mtl-2 is not expressed in nematodes in which elt-2 has been disrupted [2].
• Purification, characterization, and cDNA cloning of a novel metallothionein-like, cadmium-binding protein from Caenorhabditis elegans [3].
• The amino acid sequence of MT-Ce is unique, and neither its putative alpha and beta domains nor its Cys residues can be readily aligned with the corresponding regions of other eukaryotic MTs [3].

Biological context of mtl-2

• No measurable compensatory up-regulation of mtl-l could be observed in the null allele of mtl-2, suggesting that both isoforms are independent and not synergistic in their mode of action [4].
• This suggests the possibilities of regulation by alternative splicing and/or the presence of multiple MT-Ce genes encoding a single protein, but controlled by different regulatory elements [3].
• Caenorhabditis elegans adapted for survival in high concentrations of Cd(II) express a heavy metal binding protein designated C. elegans metallothionein-like protein or MT-Ce [3].
• Subsequently, cloned cDNAs, corresponding to MT-Ce mRNA sequences, were isolated from a lambda ZapII cDNA library prepared from the enriched template mRNA. cDNA and protein sequence analysis revealed that MT-Ce comprises 62 amino acid residues and has a predicted Mr of 6462 [3].
• The genome of the nematode Caenorhabditis elegans contains two metallothionein genes, both involved in metal homeostasis and/or detoxification [5].

Associations of mtl-2 with chemical compounds

• A radiolabeled 41-mer oligonucleotide, designed from the partial MT-Ce sequence, was used in conjunction with sucrose gradient centrifugation to obtain size-fractionated poly(A+) RNA enriched in MT-Ce sequences [3].
• Other genes induced across most timepoints included lipoxygenase, calmodulin, phospholipase C, metallothionein-like protein, and chalcone reductase [6].

Other interactions of mtl-2

• In vivo deletion and site-directed mutation analyses confirm that one GATA element in mtl-1 and two in mtl-2 are required for transcription [2].

References