Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea - PubMed (original) (raw)

Review

Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea

Abu Iftiaf Md Salah Ud-Din et al. Cell Mol Life Sci. 2017 Sep.

Abstract

Chemotaxis is the directed motility by means of which microbes sense chemical cues and relocate towards more favorable environments. Methyl-accepting chemotaxis proteins (MCPs) are the most common receptors in bacteria and archaea. They are arranged as trimers of dimers that, in turn, form hexagonal arrays in the cytoplasmic membrane or in the cytoplasm. Several different classes of MCPs have been identified according to their ligand binding region and membrane topology. MCPs have been further classified based on the length and sequence conservation of their cytoplasmic domains. Clusters of membrane-embedded MCPs often localize to the poles of the cell, whereas cytoplasmic MCPs can be targeted to the poles or distributed throughout the cell body. MCPs play an important role in cell survival, pathogenesis, and biodegradation. Bacterial adaptation to diverse environmental conditions promotes diversity among the MCPs. This review summarizes structure, classification, and structure-activity relationship of the known MCP receptors, with a brief overview of the signal transduction mechanisms in bacteria and archaea.

Keywords: Chemoreceptor, ligand-binding domain; Protein structure; Sensory domain; Signaling domain; Structure–activity relationship.

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Conflict of interest statement

The authors have no conflict interest.

Figures

Fig. 1

Fig. 1

Overall topology of typical methyl-accepting chemotaxis protein. LBD ligand binding domain, TM transmembrane helix, CC control cable, HAMP histidine kinase, adenyl cyclase, methyl-accepting chemotaxis protein and phosphatase region, PS phase stutter, SD signaling domain, MH methylation helix, FB flexible bundle, SSD signaling subdomain

Fig. 2

Fig. 2

Classification of methyl-accepting chemotaxis proteins based on membrane topology and LBD. The larger size of the LBD represents the longer amino acid sequence

Fig. 3

Fig. 3

Seven major classes of cytoplasmic signaling domains of methyl-accepting chemotaxis proteins. The methylation bundle, flexible bundle, and signaling subdomain are colored green, purple, and blue, respectively. Each box represents two heptads. The names of MCP classes were assigned according to the number of heptads (24–44 H) [27]

Fig. 4

Fig. 4

Signal recognition and transduction mechanism by a typical MCP receptor in bacteria

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