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RepA-WH1 prionoid: Clues from bacteria on factors governing phase transitions in amyloidogenesis

AuthorsGiraldo, R. ; Fernández, Cristina; Moreno-del Álamo, María ; Molina-García, Laura ; Revilla-García, Aída; Sánchez-Martínez, María Cruz; Giménez-Abián, Juan F. ; Moreno Díaz de la Espina, Susana
KeywordsAmyloid proteinopathy
Amyloid polymorphism
Bacterial prionoid
Hsp70 chaperone
Phase transitions
Issue Date4-Apr-2016
PublisherTaylor & Francis
CitationPrion, 10:41–49 ( 2016)
AbstractIn bacterial plasmids, Rep proteins initiate DNA replication by undergoing a structural transformation coupled to dimer dissociation. Amyloidogenesis of the ‘winged-helix’ N-terminal domain of RepA (WH1) is triggered in vitro upon binding to plasmid-specific DNA sequences, and occurs at the bacterial nucleoid in vivo. Amyloid fibers are made of distorted RepA-WH1 monomers that assemble as single or double intertwined tubular protofilaments. RepA-WH1 causes in E. coli an amyloid proteinopathy, which is transmissible from mother to daughter cells, but not infectious, and enables conformational imprinting in vitro and in vivo; i.e. RepA-WH1 is a ‘prionoid’. Microfluidics allow the assessment of the intracellular dynamics of RepA-WH1: bacterial lineages maintain two types (strains-like) of RepA-WH1 amyloids, either multiple compact cytotoxic particles or a single aggregate with the appearance of a fluidized hydrogel that it is mildly detrimental to growth. The Hsp70 chaperone DnaK governs the phase transition between both types of RepA-WH1 aggregates in vivo, thus modulating the vertical propagation of the prionoid. Engineering chimeras between the Sup35p/[PSI*] prion and RepA-WH1 generates [REP-PSI*], a synthetic prion exhibiting strong and weak phenotypic variants in yeast. These recent findings on a synthetic, self-contained bacterial prionoid illuminate central issues of protein amyloidogenesis.
Description10 p.-1 fig.
Publisher version (URL)http://dx.doi.org/10.1080/19336896.2015.1129479
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