Rifampicin supersensitivity of rho strains of E. coli, and suppression by sur mutation
Escherichia coli strains with mutations rho-115, rho-ts15, rho-101 (psu-1) or rho-102 (psu-2) are more sensitive ("supersensitive") to rifampicin than isogenic parent strains, as measured by growth rate in broth and colony forming efficiency on solid media with 5, 10, or 20 microgram of ri...
Saved in:
Published in | Molecular & general genetics Vol. 169; no. 1; p. 27 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Germany
16.01.1979
|
Subjects | |
Online Access | Get more information |
Cover
Loading…
Summary: | Escherichia coli strains with mutations rho-115, rho-ts15, rho-101 (psu-1) or rho-102 (psu-2) are more sensitive ("supersensitive") to rifampicin than isogenic parent strains, as measured by growth rate in broth and colony forming efficiency on solid media with 5, 10, or 20 microgram of rifampicin per ml. There is no change in sensitivity of rho mutants to the antibiotics penicillin, erythromycin, chloramphenicol, or the detergent desoxycholate. The rho-101 or rho-102 mutations confer rifampicin supersensitivity at 32 degrees C but not 42 degrees C. Mutants of a rho-115 strain that have lost polarity suppression can be isolated by selection for rifampicin resistance. This phenotype, Sur, is not due to reversion of the original rho gene mutation but to a second mutation perhaps in the gene for rho protein or the gene for the beta subunit of RNA polymerase. One class of Sur mutation, occurring in rho-115 cells isolated as resistant to 20 microgram of rifampicin per ml, is co-transducible with the marker ilv, and the gene order is rbs-ilv-sur-38. A model suggested by this map position is that the mutations rho-115 and sur-38 define the domain of rho protein which interacts with the beta subunit of RNA polymerase. |
---|---|
ISSN: | 0026-8925 |
DOI: | 10.1007/BF00267541 |