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Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function.

Abstract
Lack of molybdenum cofactor (MoCo) in Escherichia coli and related microorganisms was found to cause hypersensitivity to certain N-hydroxylated base analogs, such as HAP (6-N-hydroxylaminopurine). This observation has lead to a previous proposal that E. coli contains a molybdoenzyme capable of detoxifying such N-hydroxylated analogs. Here, we show that, unexpectedly, deletion of all known or putative molybdoenzymes in E. coli failed to reveal any base-analog sensitivity, suggesting that a novel type of MoCo-dependent activity is involved. Further, we establish that protection against the analogs does not require the common molybdopterin guanine-dinucleotide (MGD) form of the cofactor, but instead the guanosine monophosphate (GMP)-free version of MoCo (MPT) is sufficient.
AuthorsStanislav G Kozmin, Roel M Schaaper
JournalMutation research (Mutat Res) Vol. 619 Issue 1-2 Pg. 9-15 (Jun 01 2007) ISSN: 0027-5107 [Print] Netherlands
PMID17349664 (Publication Type: Journal Article, Research Support, N.I.H., Intramural)
Chemical References
  • Coenzymes
  • Escherichia coli Proteins
  • Metalloproteins
  • Molybdenum Cofactors
  • Mutagens
  • Pteridines
  • mobA protein, E coli
  • 6-N-hydroxylaminopurine
  • molybdenum cofactor
  • Adenine
Topics
  • Adenine (analogs & derivatives, toxicity)
  • Coenzymes (chemistry, metabolism)
  • Drug Resistance, Bacterial (genetics)
  • Escherichia coli (drug effects, genetics, metabolism)
  • Escherichia coli Proteins (genetics, metabolism)
  • Genes, Bacterial
  • Metalloproteins (chemistry, metabolism)
  • Molybdenum Cofactors
  • Mutagens (toxicity)
  • Pteridines (chemistry, metabolism)

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