ParP prevents dissociation of CheA from chemotactic signaling arrays and tethers them to a polar anchor

Ringgaard, Simon; Zepeda-Rivera, Martha A.; Wu, Xiumei; Schirner, Kathrin; Davis, Brigid M.; Waldor, Matthew K.

doi:10.1073/pnas.1315722111

Cited by 46 publications

(94 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is also possible that CheV1 or CheW have additional interactions beyond chemotaxis proteins, similar to the ParP protein from Vibrio parahaemolyticus (47). ParP, like CheV1, is a hybrid protein with a CheW-like domain.…”

Section: Discussionmentioning

confidence: 99%

“…Like CheV1, ParP mutants have decreased soft agar migration and are more smooth swimming than wild type (9,19,40). ParP interacts with CheA and a membrane protein called ParC, and stabilizes chemotaxis complexes at the cell pole by preventing CheA dissociation (47). A common theme is the use of the CheW domain as a connection point for protein-protein interactions either between arrays or with other proteins.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Cooperation of two distinct coupling proteins creates chemosensory network connections

Abedrabbo

Castellon

Collins

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Although it is appreciated that bacterial chemotaxis systems rely on coupling, also called scaffold, proteins to both connect input receptors with output kinases and build interkinase connections that allow signal amplification, it is not yet clear why many systems use more than one coupling protein. We examined the distinct functions for multiple coupling proteins in the bacterial chemotaxis system of Helicobacter pylori, which requires two nonredundant coupling proteins for chemotaxis: CheW and CheV1, a hybrid of a CheW and a phosphorylatable receiver domain. We report that CheV1 and CheW have largely redundant abilities to interact with chemoreceptors and the CheA kinase, and both similarly activated CheA’s kinase activity. We discovered, however, that they are not redundant for formation of the higher order chemoreceptor arrays that are known to form via CheA–CheW interactions. In support of this possibility, we found that CheW and CheV1 interact with each other and with CheA independent of the chemoreceptors. Therefore, it seems that some microbes have modified array formation to require CheW and CheV1. Our data suggest that multiple coupling proteins may be used to provide flexibility in the chemoreceptor array formation.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cooperation of two distinct coupling proteins creates chemosensory network connections

Abedrabbo

Castellon

Collins

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Additional PpfA interactions with chromosomal DNA may fix the cluster localization and allow the cluster to be segregated during cell division with chromosomal DNA (69). This localization mechanism may be widespread, given that many cytoplasmic chemoreceptors are encoded in the same operon as a protein with PpfA homology (46), and positioning of chemosensory arrays in Vibrio also seems to depend on the presence and activity of a ParA-like protein, ParC (70,71).…”

Section: Cytoplasmic Chemoreceptors That Form Clusters Distinct From mentioning

confidence: 99%

Internal Sense of Direction: Sensing and Signaling from Cytoplasmic Chemoreceptors

Collins

Lacal

Ottemann

2014

Microbiol Mol Biol Rev

View full text Add to dashboard Cite

SUMMARY Chemoreceptors sense environmental signals and drive chemotactic responses in Bacteria and Archaea . There are two main classes of chemoreceptors: integral inner membrane and soluble cytoplasmic proteins. The latter were identified more recently than integral membrane chemoreceptors and have been studied much less thoroughly. These cytoplasmic chemoreceptors are the subject of this review. Our analysis determined that 14% of bacterial and 43% of archaeal chemoreceptors are cytoplasmic, based on currently sequenced genomes. Cytoplasmic chemoreceptors appear to share the same key structural features as integral membrane chemoreceptors, including the formations of homodimers, trimers of dimers, and 12-nm hexagonal arrays within the cell. Cytoplasmic chemoreceptors exhibit varied subcellular locations, with some localizing to the poles and others appearing both cytoplasmic and polar. Some cytoplasmic chemoreceptors adopt more exotic locations, including the formations of exclusively internal clusters or moving dynamic clusters that coalesce at points of contact with other cells. Cytoplasmic chemoreceptors presumably sense signals within the cytoplasm and bear diverse signal input domains that are mostly N terminal to the domain that defines chemoreceptors, the so-called MA domain. Similar to the case for transmembrane receptors, our analysis suggests that the most common signal input domain is the PAS (Per-Arnt-Sim) domain, but a variety of other N-terminal domains exist. It is also common, however, for cytoplasmic chemoreceptors to have C-terminal domains that may function for signal input. The most common of these is the recently identified chemoreceptor zinc binding (CZB) domain, found in 8% of all cytoplasmic chemoreceptors. The widespread nature and diverse signal input domains suggest that these chemoreceptors can monitor a variety of cytoplasmically based signals, most of which remain to be determined.

show abstract

“…Fluorescence microscopy was done essentially as described previously (23,34), with a few modifications. For microscopy, 200 μL of an overnight culture of V. cholerae harboring plasmid pPM064 for expression of CheW0-YFP was added to 10 mL of LB medium supplemented with 200 μg/mL streptomycin and 5 μg/mL chloramphenicol, followed by incubation at 30°C with shaking.…”

Section: Methodsmentioning

confidence: 99%

Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM

Briegel

Ortega

Mann

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Nearly all motile bacterial cells use a highly sensitive and adaptable sensory system to detect changes in nutrient concentrations in the environment and guide their movements toward attractants and away from repellents. The best-studied bacterial chemoreceptor arrays are membrane-bound. Many motile bacteria contain one or more additional, sometimes purely cytoplasmic, chemoreceptor systems. Vibrio cholerae contains three chemotaxis clusters (I, II, and III). Here, using electron cryotomography, we explore V. cholerae's cytoplasmic chemoreceptor array and establish that it is formed by proteins from cluster I. We further identify a chemoreceptor with an unusual domain architecture, DosM, which is essential for formation of the cytoplasmic arrays. DosM contains two signaling domains and spans the two-layered cytoplasmic arrays. Finally, we present evidence suggesting that this type of receptor is important for the structural stability of the cytoplasmic array.chemotaxis | chemoreceptor arrays | Vibrio cholerae | electron cryotomography | microscopy M ost motile bacteria move toward favorable environments through a process called chemotaxis. The molecular basis of this behavior is best understood in Escherichia coli, where transmembrane methyl-accepting chemotaxis proteins (MCPs, or chemoreceptors) form large arrays at the cell pole. The chemoreceptors bind attractants or repellents in the periplasm (1-3) and relay signals to histidine kinases (CheA) in the cytoplasm (4). When activated, CheA first autophosphorylates and then transfers the phosphoryl group to the response regulators CheY and CheB. Phosphorylated CheY binds to the flagellar motor, changing the direction of flagellar rotation. This allows the cells to switch from swimming forward smoothly (so-called "runs") to tumbling randomly. Changes in the duration and frequency of run and tumble phases drive a biased random walk that moves the cells toward favorable environments (5). The other response regulator, CheB, is a methylesterase, which, in conjunction with the constitutively active methyltransferase CheR, tunes the sensitivity of the system by changing the methylation state of the chemoreceptors (6-8).Although there is only one chemotaxis system in E. coli, most chemotactic bacterial and archaeal species have multiple systems (9). For instance, Rhodobacter sphaeroides has three chemotaxis systems encoded in three distinct clusters of genes, one of which (CheOp2) encodes two receptors without predicted transmembrane domains, TlpT and TlpC (10). Analysis of fluorescently tagged TlpT and TlpC revealed that they localize in foci around midcell. The foci split before cell division and are segregated to the midcell position within the future daughter cells. The chromosome-associated ParA-like ATPase PpfA controls the localization and segregation of the foci through an interaction with the N terminus of TlpT in a ParB-like manner (11).Using electron cryotomography (ECT), we discovered that these cytoplasmic foci in R. sphaerodes are ordered arrays of chemore...

show abstract

ParP prevents dissociation of CheA from chemotactic signaling arrays and tethers them to a polar anchor

Cited by 46 publications

References 44 publications

Cooperation of two distinct coupling proteins creates chemosensory network connections

Cooperation of two distinct coupling proteins creates chemosensory network connections

Internal Sense of Direction: Sensing and Signaling from Cytoplasmic Chemoreceptors

Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM

Contact Info

Product

Resources

About