TY - JOUR
T1 - Identification of a novel transcription regulator from Proteus mirabilis, PMTR, revealed a possible role of YJAI protein in balancing zinc in Escherichia coli
AU - Noll, Meenakshi
AU - Petrukhin, Konstantin
AU - Lutsenko, Svetlana
PY - 1998/8/14
Y1 - 1998/8/14
N2 - Zinc is an essential trace element required for structural integrity and functional activity of numerous proteins, yet mechanisms by which cells regulate zinc concentration are poorly understood. Here, we identified a gene from Proteus mirabilis that encodes a 135-amino acid residue protein, PMTR (P. mirabilis transcription regulator), a new member of the MerR family of transcription activators. Transformation of Escherichia coli with PMTR- carrying vectors specifically increases cell tolerance to zinc, suggesting the role of PMTR in zinc homeostasis. In response to zinc, PMTR-containing cells robustly accumulate a 12-kDa protein, the amount of which correlates with the cells' ability to grow at high zinc concentrations. The 12-kDa protein is not induced in the presence of Ni2+, Co2+, Cd2+, Mn2+, or Fe2+, indicating that the PMTR-dependent expression of the 12kDa protein is specifically regulated by zinc. The 12-kDa protein was identified as the C- terminal fragment of E. coli protein YJAI, and was shown to contain two zinc- binding motifs. Metal-affinity chromatography and 65Zn blotting assay confirmed the ability of the 12-kDa protein to bind zinc specifically (zinc > cobalt >> cadmium). We propose that YJAI is an important component of the zinc-balancing mechanism in E. coli, the up-regulation of which with PMTR results in an increased tolerance to zinc.
AB - Zinc is an essential trace element required for structural integrity and functional activity of numerous proteins, yet mechanisms by which cells regulate zinc concentration are poorly understood. Here, we identified a gene from Proteus mirabilis that encodes a 135-amino acid residue protein, PMTR (P. mirabilis transcription regulator), a new member of the MerR family of transcription activators. Transformation of Escherichia coli with PMTR- carrying vectors specifically increases cell tolerance to zinc, suggesting the role of PMTR in zinc homeostasis. In response to zinc, PMTR-containing cells robustly accumulate a 12-kDa protein, the amount of which correlates with the cells' ability to grow at high zinc concentrations. The 12-kDa protein is not induced in the presence of Ni2+, Co2+, Cd2+, Mn2+, or Fe2+, indicating that the PMTR-dependent expression of the 12kDa protein is specifically regulated by zinc. The 12-kDa protein was identified as the C- terminal fragment of E. coli protein YJAI, and was shown to contain two zinc- binding motifs. Metal-affinity chromatography and 65Zn blotting assay confirmed the ability of the 12-kDa protein to bind zinc specifically (zinc > cobalt >> cadmium). We propose that YJAI is an important component of the zinc-balancing mechanism in E. coli, the up-regulation of which with PMTR results in an increased tolerance to zinc.
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U2 - 10.1074/jbc.273.33.21393
DO - 10.1074/jbc.273.33.21393
M3 - Article
C2 - 9694902
AN - SCOPUS:0032516844
SN - 0021-9258
VL - 273
SP - 21393
EP - 21401
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 33
ER -