scholarly journals Glutamyl-γ-methyl ester acts as a methionine analogue inEscherichia coli: analogue resistant mutants map at themetJandmetKloci

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.

2004 ◽  
Vol 186 (13) ◽  
pp. 4402-4406 ◽  
Author(s):  
Volkmar Braun ◽  
Christina Herrmann

ABSTRACT Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.


1976 ◽  
Vol 66 (2) ◽  
pp. 369-377 ◽  
Author(s):  
Peter PREHM ◽  
Stephan STIRM ◽  
Barbara JANN ◽  
Klaus JANN ◽  
Hans G. BOMAN

1979 ◽  
Vol 34 (2) ◽  
pp. 121-130 ◽  
Author(s):  
Mahavir Singh ◽  
Umakant Sinha

SUMMARYFour recessive amino-acid-analogue-resistant mutants were isolated on a medium containing acetate as the sole carbon source and the amino acid analogues p-fluorophenylalanine and ethionine. None of the mutants showed any growth requirement. Analysis of growth on media containing an amino acid as the sole nitrogen source indicated that two mutants out of the four possess normal systems for utilization of acidic, neutral, basic and aromatic amino acids. The mutantsfpa70 andfpa71 showed reduced growth on tryptophan as the sole source of nitrogen. Three new loci, identified after preliminary genetic analysis, were located on three linkage groups: one each on linkage groups I, VI and VIII.


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