Source:http://linkedlifedata.com/resource/pubmed/id/19575436
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2009-10-26
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pubmed:abstractText |
The effects of CdSO(4) additions on the gene expressions of a mercury reductase, merA, an oxidative stress protein, trxA, the ammonia-monooxygenase enzyme (AMO), amoA, and the hydroxylamine oxidoreductase enzyme (HAO), hao, were examined in continuously cultured N. europaea cells. The reactor was fed 50 mM NH(4)+ and was operated for 78 days with a 6.9 days hydraulic retention time. Over this period, six successive batch additions of CdSO(4) were made with increasing maximum concentrations ranging from 1 to 60 microM Cd(2+). The expression of merA was highly correlated with the level of Cd(2+) within the reactor (Rs = 0.90) with significant up-regulation measured at non-inhibitory Cd(2+) concentrations. Cd(2+) appears to target AMO specifically at lower concentrations and caused oxidative stress at higher concentrations, as indicated by the SOURs (specific oxygen uptake rates) and the up-regulation of trxA. Since Cd(2+) inhibition is irreversible and amoA was up-regulated in response to Cd(2+) inhibition, it is hypothesized that de novo synthesis of the AMO enzyme occurred and was responsible for the observed recovery in activity. Continuously cultured N. europaea cells were more resistant to Cd(2+) inhibition than previously examined batch cultured cells due to the presence of Mg(2+) and Ca(2+) in the growth media, suggesting that Cd(2+) enters the cell through Mg(2+) and Ca(2+) import channels. The up-regulation of merA during exposure to non-inhibitory Cd(2+) levels indicates that merA is an excellent early warning signal for Cd(2+) inhibition.
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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/Cadmium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Quaternary Ammonium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/ammonia monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/cadmium sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/hydroxylamine oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/mercuric reductase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1097-0290
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1004-11
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pubmed:meshHeading |
pubmed-meshheading:19575436-Bacterial Proteins,
pubmed-meshheading:19575436-Bioreactors,
pubmed-meshheading:19575436-Cadmium Compounds,
pubmed-meshheading:19575436-Gene Expression Profiling,
pubmed-meshheading:19575436-Gene Expression Regulation, Bacterial,
pubmed-meshheading:19575436-Nitrosomonas europaea,
pubmed-meshheading:19575436-Oxidoreductases,
pubmed-meshheading:19575436-Quaternary Ammonium Compounds,
pubmed-meshheading:19575436-Stress, Physiological,
pubmed-meshheading:19575436-Sulfates,
pubmed-meshheading:19575436-Thioredoxins
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pubmed:year |
2009
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pubmed:articleTitle |
Expression of merA, trxA, amoA, and hao in continuously cultured Nitrosomonas europaea cells exposed to cadmium sulfate additions.
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pubmed:affiliation |
School of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, Oregon 97331-3212, USA. tyler.radniecki@oregonstate.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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