Specificity of subtilin-mediated activation of histidine kinase SpaK.

Specificity of subtilin-mediated activation of histidine kinase SpaK. Appl Environ Microbiol. 2017 Jul 14;: Authors: Geiger C, Spieß T, Korn SM, Kötter P, Entian KD Abstract Autoinduction via two-component systems is a widespread regulatory mechanism that senses environmental and metabolic changes. Although the lantibiotics nisin and subtilin are closely related and share the same lanthionine ring structure, they autoinduce their biosynthesis in a highly specific manner. Subtilin can only activate the two-component system SpaRK of Bacillus subtilis, whereas nisin activates solely the two-component system NisRK of Lactococcus lactis To identify components that determine the specificity of subtilin autoinduction, several variants of the respective lantibiotic were analyzed for their autoinduction capacity. In here we show that amino acid position 20 is crucial for SpaK activation as an engineered nisin molecule with phenylalanine at position 20 (nisin N20F) was able to activate SpaK in a specific manner. In combination with the N-terminal tryptophan of subtilin (nisin I1W/N20F) SpaK autoinduction reached almost the level of subtilin mediated autoinduction. Furthermore, the overall structure of subtilin is also important for its association with the histidine kinase. Destruction of the second lanthionine ring (subtilin C11A, ring B) as well as mutations which interfere with the flexibility of the hinge region located between lanthioni...
Source: Applied and Environmental Microbiology - Category: Microbiology Authors: Tags: Appl Environ Microbiol Source Type: research