In:
Molecular Microbiology, Wiley, Vol. 97, No. 6 ( 2015-09), p. 1063-1078
Abstract:
Chemotaxis is important for H elicobacter pylori to colonize the stomach. Like other bacteria, H . pylori uses chemoreceptors and conserved chemotaxis proteins to phosphorylate the flagellar rotational response regulator, C he Y , and modulate the flagellar rotational direction. Phosphorylated C he Y is returned to its non‐phosphorylated state by phosphatases such as C he Z . In previously studied cases, chemotaxis phosphatases localize to the cellular poles by interactions with either the C he A chemotaxis kinase or flagellar motor proteins. We report here that the H . pylori C he Z , C he Z HP , localizes to the poles independently of the flagellar motor, C he A , and all typical chemotaxis proteins. Instead, C he Z HP localization depends on the chemotaxis regulatory protein C he P ep, and reciprocally, C he P ep requires C he Z HP for its polar localization. We furthermore show that these proteins interact directly. Functional domain mapping of C he Z HP determined the polar localization motif lies within the central domain of the protein and that the protein has regions outside of the active site that participate in chemotaxis. Our results suggest that C he Z HP and C he P ep form a distinct complex. These results therefore suggest the intriguing idea that some phosphatases localize independently of the other chemotaxis and motility proteins, possibly to confer unique regulation on these proteins' activities.
Type of Medium:
Online Resource
ISSN:
0950-382X
,
1365-2958
DOI:
10.1111/mmi.2015.97.issue-6
Language:
English
Publisher:
Wiley
Publication Date:
2015
detail.hit.zdb_id:
1501537-3
