Molybdenum Cofactor-dependent Resistance to N-hydroxylated Base Analogs in Escherichia Coli is Independent of MobA Function

Overview

Journal Mutat Res

Publisher Elsevier

Specialty Genetics

Date 2007 Mar 14

PMID 17349664

Citations 22

Authors

Stanislav G Kozmin

Roel M Schaaper

Affiliations

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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.

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