Biological Diversity and Molecular Plasticity of FIC Domain Proteins

Harms, Alexander and Stanger, Frédéric Valentin and Dehio, Christoph. (2016) Biological Diversity and Molecular Plasticity of FIC Domain Proteins. Annual Reviews of Microbiology, 70. pp. 341-360.

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The ubiquitous proteins with FIC (filamentation induced by cyclic AMP) domains use a conserved enzymatic machinery to modulate the activity of various target proteins by posttranslational modification, typically AMPylation. Following intensive study of the general properties of FIC domain catalysis, diverse molecular activities and biological functions of these remarkably versatile proteins are now being revealed. Here, we review the biological diversity of FIC domain proteins and summarize the underlying structure-function relationships. The original and most abundant genuine bacterial FIC domain proteins are toxins that use diverse molecular activities to interfere with bacterial physiology in various, yet ill-defined, biological contexts. Host-targeted virulence factors have evolved repeatedly out of this pool by exaptation of the enzymatic FIC domain machinery for the manipulation of host cell signaling in favor of bacterial pathogens. The single human FIC domain protein HypE (FICD) has a specific function in the regulation of protein stress responses.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Molecular Microbiology (Dehio)
UniBasel Contributors:Dehio, Christoph and Harms, Alexander
Item Type:Article, refereed
Article Subtype:Book Review
Publisher:Annual Reviews
Note:Publication type according to Uni Basel Research Database: Journal item
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Last Modified:20 May 2020 03:10
Deposited On:27 Oct 2017 12:40

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