Methionine and glutamine transport systems in D-methionine utilising revertants of Salmonella typhimurium

✍ Scribed by Poland, J. ;Ayling, P. D.

• Publisher: Springer
• Year: 1984
• Tongue: English
• Weight: 927 KB
• Volume: 194
• Category: Article
• ISSN: 0026-8925
• DOI: 10.1007/bf00383520

✦ Synopsis

In Salmonella typhimurium, methionine auxotrophs such as metB can use D-methionine as a methionine source. MetP mutations prevent this growth since D-methionine can enter only via the metP high-affinity methionine transport system. D-methionine utilising revertants ( Dmu +) were selected from metB23 metP760 ( HU76 ) following nitrosoguanidine mutagenesis. The properties of two such revertants, HU206 and HU415 , indicated that reversion was not due to backmutation of the metP760 mutation. Genetic analysis indicated that each strain possessed two mutations, designated dmu and gln, in addition to the original metB23 and metP760 mutations. The dmu mutation restores ability to grow on D-methionine, partly restores D- and L-methionine transport activity, and makes the cells particularly sensitive to inhibition by L-glutamine while growing on D but not L-methionine. The growth inhibition by L-glutamine was shown to be caused by competition by L-glutamine for D-methionine transport by the high-affinity methionine system. The gln mutation greatly reduces activity of the high-affinity glutamine transport system. The Dmu + strains are also partly defective in the glutamine low-affinity transport system, possibly because the partially-restored methionine high-affinity system, or a component of tis system, functions in the transport of glutamine by its low-affinity system.