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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
1998-9-14
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pubmed:abstractText |
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 12-kDa 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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21393-401
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9694902-Amino Acid Sequence,
pubmed-meshheading:9694902-Bacterial Proteins,
pubmed-meshheading:9694902-Base Sequence,
pubmed-meshheading:9694902-DNA, Bacterial,
pubmed-meshheading:9694902-Escherichia coli,
pubmed-meshheading:9694902-Escherichia coli Proteins,
pubmed-meshheading:9694902-Molecular Sequence Data,
pubmed-meshheading:9694902-Protein Binding,
pubmed-meshheading:9694902-Proteus mirabilis,
pubmed-meshheading:9694902-Sequence Homology, Amino Acid,
pubmed-meshheading:9694902-Subcellular Fractions,
pubmed-meshheading:9694902-Trans-Activators,
pubmed-meshheading:9694902-Zinc
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pubmed:year |
1998
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pubmed:articleTitle |
Identification of a novel transcription regulator from Proteus mirabilis, PMTR, revealed a possible role of YJAI protein in balancing zinc in Escherichia coli.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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