scholarly journals Chromosomal location of a mutation causing chloramphenicol resistance in Escherichia coli K 12

1968 ◽  
Vol 11 (1) ◽  
pp. 97-104 ◽  
Author(s):  
E. C. R. Reeve ◽  
D. R. Suttie

A chloramphenicol-resistant mutation in Escherichia coli K 12, cmlA1 (previously designated 1a), giving a higher Cm-resistance than other mutations yet examined, has been shown to have a chromosomal location, the gene order being gal, λ, bio, cmlA, pyrD. CmlA can be transduced efficiently into cm-sensitive strains by P1 with little phenotypic lag, and is co-transduced with the λ-attachment site (frequency 1·13%) but not with gal or pyrD.

1979 ◽  
Vol 29 (2) ◽  
pp. 808-810 ◽  
Author(s):  
A P Pugsley ◽  
D Littmann-Louth ◽  
C A Schnaitman

2008 ◽  
Vol 190 (10) ◽  
pp. 3670-3680 ◽  
Author(s):  
Yoshikane Itoh ◽  
John D. Rice ◽  
Carlos Goller ◽  
Archana Pannuri ◽  
Jeannette Taylor ◽  
...  

ABSTRACT The linear homopolymer poly-β-1,6-N-acetyl-d-glucosamine (β-1,6-GlcNAc; PGA) serves as an adhesin for the maintenance of biofilm structural stability in diverse eubacteria. Its function in Escherichia coli K-12 requires the gene products of the pgaABCD operon, all of which are necessary for biofilm formation. PgaC is an apparent glycosyltransferase that is required for PGA synthesis. Using a monoclonal antibody directed against E. coli PGA, we now demonstrate that PgaD is also needed for PGA formation. The deletion of genes for the predicted outer membrane proteins PgaA and PgaB did not prevent PGA synthesis but did block its export, as shown by the results of immunoelectron microscopy (IEM) and antibody adsorption assays. IEM also revealed a conditional localization of PGA at the cell poles, the initial attachment site for biofilm formation. PgaA contains a predicted β-barrel porin and a superhelical domain containing tetratricopeptide repeats, which may mediate protein-protein interactions, implying that it forms the outer membrane secretin for PGA. PgaB contains predicted carbohydrate binding and polysaccharide N-deacetylase domains. The overexpression of pgaB increased the primary amine content (glucosamine) of PGA. Site-directed mutations targeting the N-deacetylase catalytic activity of PgaB blocked PGA export and biofilm formation, implying that N-deacetylation promotes PGA export through the PgaA porin. The results of previous studies indicated that N-deacetylation of β-1,6-GlcNAc in Staphylococcus epidermidis by the PgaB homolog, IcaB, anchors it to the cell surface. The deletion of icaB resulted in release of β-1,6-GlcNAc into the growth medium. Thus, covalent modification of β-1,6-GlcNAc by N-deacetylation serves distinct biological functions in gram-negative and gram-positive species, dictated by cell envelope differences.


1965 ◽  
Vol 6 (2) ◽  
pp. 310-315 ◽  
Author(s):  
E. C. R. Reeve ◽  
J. O. Bishop

Chloramphenicol (CM), Aureomycin (AM) and Puromycin (PM) induce RNA synthesis in RC-stringent Escherichia coli starved of a required amino acid. This fact has been used to develop a method for comparing the levels of resistance of single-step CM-r mutants to the three antibiotics. Three levels of resistance to each antibiotic were found among four mutants selected in a single CM-s strain. The mutant with the highest CM resistance has the lowest AM resistance, and vice versa, while the level of PM resistance was not correlated with that of either CM or AM. The four mutants all differed from each other in their patterns of resistance to the three antibiotics.


1979 ◽  
Vol 33 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Jan Kraus ◽  
Dieter Soll ◽  
K. Brooks Low

SUMMARYEscherichia coliK-12 mutants resistant to glutamyl-γ-methyl ester were isolated. A mutation leading to resistance of up to 1·4 mg/ml of the methionine analogue maps at min 63 and is 13% cotransducible withserAindicating an alteration in themetKgene. Another mutation leading to resistance to 3 mg/ml of the analogue and cross-resistance to other amino acid analogues maps at min 87. This mutation, which has the phenotype of MetJ−, is shown to be situated between theglpKandmetBgenes and thus indicates a different gene order from the published one.


Genetics ◽  
1989 ◽  
Vol 122 (2) ◽  
pp. 279-296 ◽  
Author(s):  
E A Raleigh ◽  
R Trimarchi ◽  
H Revel

Abstract We have genetically analyzed, cloned and physically mapped the modified cytosine-specific restriction determinants mcrA (rglA) and mcrB (rglB) of Escherichia coli K-12. The independently discovered Rgl and Mcr restriction systems are shown to be identical by three criteria: 1) mutants with the RglA- or RglB- phenotypes display the corresponding McrA- or McrB- phenotypes, and vice versa; 2) the gene(s) for RglA and McrA reside together at one locus, while gene(s) for RglB and McrB are coincident at a different locus; and 3) RglA+ and RglB+ recombinant clones complement for the corresponding Mcr-deficient lesions. The mcrA (rglA) gene(s) is on the excisable element e14, just clockwise of purB at 25 min. The mcrB (rglB) gene(s), at 99 min, is in a cluster of restriction functions that includes hsd and mrr, determinants of host-specific restriction (EcoK) and methyladenine-specific restriction respectively. Gene order is mcrB-hsdS-hsdM-hsdR-mrr-serB. Possible models for the acqusition of these restriction determinants by enteric bacteria are discussed.


1999 ◽  
Vol 181 (21) ◽  
pp. 6822-6827 ◽  
Author(s):  
Keiko Kita ◽  
Junko Tsuda ◽  
Toshinobu Kato ◽  
Kenji Okamoto ◽  
Hideshi Yanase ◽  
...  

ABSTRACT A DNA fragment carrying the genes coding for EcoO109I endonuclease and EcoO109I methylase, which recognize the nucleotide sequence 5′-(A/G)GGNCC(C/T)-3′, was cloned from the chromosomal DNA of Escherichia coli H709c. TheEcoO109I restriction-modification (R-M) system was found to be inserted between the int and psu genes from satellite bacteriophage P4, which were lysogenized in the chromosome at the P4 phage attachment site of the corresponding leuX gene observed in E. coli K-12 chromosomal DNA. Thesid gene of the prophage was inactivated by insertion of one copy of IS21. These findings may shed light on the horizontal transfer and stable maintenance of the R-M system.


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