Abstract:
:MarR, the negative regulator of the Escherichia coli multiple antibiotic resistance (marRAB) operon, is a member of a newly recognized family of regulatory proteins. The amino acid sequences of these proteins do not display any apparent homologies to the DNA binding domains of prokaryotic transcription regulators and a DNA binding motif for any one of the MarR homologues is currently unknown. In order to define regions of MarR required for DNA binding, mutant repressors, selected based on their ability to interfere with (negatively complement) the activity of wild-type MarR, were isolated. As determined using gel mobility shift assays, 13 out of 14 negative complementing mutants tested were unable to bind DNA in vitro. Three negative complementing alleles presumably specify truncated repressors and one of these proteins, a 120 residue MarR, can bind DNA in vitro. Most of the negative complementing mutations were clustered within two areas of MarR with features related to a helix-turn-helix DNA binding motif. These regions are presumed to be required for the DNA binding activity of the repressor.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Alekshun MN,Kim YS,Levy SBdoi
10.1046/j.1365-2958.2000.01802.xsubject
Has Abstractpub_date
2000-03-01 00:00:00pages
1394-404issue
6eissn
0950-382Xissn
1365-2958pii
mmi1802journal_volume
35pub_type
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