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  • Synechococcus PCC 7942  (2)
  • 1
    ISSN: 1573-5028
    Keywords: Arabidopsis ; metallothionein-like genes ; MT2 ; smt ; Synechococcus PCC 7942
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Zn2+ proteins pervade metabolism and are essential for gene expression. However, no proteins have been ascribed the central roles of Zn2+ donation to, or removal from, metalloproteins, or Zn2+ storage in vegetative plant tissue. In animals, such functions have been proposed for metallothioneins. Plants contain multiple metallothionein-like genes but their predicted products, which differ significantly from animal metallothioneins, remain to be isolated from vegetative tissue and their roles are uncertain. The type 2 metallothionein-like gene from Arabidopsis, MT2, was expressed under the control of Zn2+-responsive elements derived from the cyanobacterial metallothionein divergon, smt. Zn2+-dependent expression of MT2 transcripts in Synechococcus PCC 7942 was confirmed by northern analysis. The Arabidopsis MT2 gene partly complemented Zn2+ hypersensitivity in mutants of Synechococcus PCC 7942 which are functionally deficient in an endogenous Zn2+-metallothionein gene, smtA. MT2 was also expressed as a recombinant fusion protein in Escherichia coli, purified and shown to bind Zn2+ in vitro. The mean pH of half displacement of Zn2+ from MT2 was estimated to be 5.05. This suggests that MT2 has a greater affinity for Zn2+ than phytochelatins. The results presented here reveal that MT2 is capable of binding Zn2+ in vitro, conferring tolerance to elevated [Zn2+] in vivo within cyanobacteria and is likely to compete with other polypeptides for cellular Zn2+ in planta.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of applied phycology 8 (1996), S. 81-82 
    ISSN: 1573-5176
    Keywords: Zn2+-metabolism ; chloroplast-translation ; evolution of tRNA synthetases ; aminoacyl-tRNA synthetase ; Synechococcus PCC 7942 ; pheT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report an open reading frame (ORF) fromSynechococcus PCC 7942 encoding a protein (812 residues) with 61% similarity (39% identity) to PheT fromBacillus subtilis. Expression of this ORF was confirmed by reverse transcriptase PCR with Southern analysis. PheT is one of the subunits of phenylalanyl-tRNA synthetase which together catalyse the ligation of phenylalanine to its cognate tRNA. This is the second gene encoding a representative of the twenty tRNA synthetases to have been isolated from cyanobacteria and fully sequenced. The key words allude to implications resulting from the isolation of this gene which have attracted our attention.
    Type of Medium: Electronic Resource
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