Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids

• Published in: Communications biology Vol. 1; no. 1; p. 52
• Main Authors: Sugimoto, Shinya, Arita-Morioka, Ken-Ichi, Terao, Akari, Yamanaka, Kunitoshi, Ogura, Teru, Mizunoe, Yoshimitsu
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.01.2018; Nature Publishing Group UK
• Subjects: Antibiotics; Bacteria; Biofilms; Biology; Biosynthesis; Colonization; DnaK protein; Hsp70 protein; Polymers; Quality control; Sigma factor; Signal peptides; Stationary phase
• ISSN: 2399-3642; 2399-3642
• DOI: 10.1038/s42003-018-0056-0

Biofilms are intricate communities of microorganisms embedded in a self-produced matrix of extracellular polymer, which provides microbes survival advantages in stressful environments and can cause chronic infections in humans. Curli are functional amyloids that assemble on the extracellular surface of enteric bacteria such as during biofilm development and colonization. The molecular chaperone DnaK, a bacterial Hsp70 homologue, promotes curli biogenesis via unknown mechanism(s). Here we show that DnaK increases the expression of CsgA and CsgB-the major and minor structural components of curli, respectively-via a quantity and quality control of RpoS, a stationary phase-specific alternative sigma factor regulating bacterial transcription, and CsgD, the master transcriptional regulator of curli formation. DnaK also keeps CsgA and CsgB in a translocation-competent state by binding to their signal peptides prone to aggregation. Our findings suggest that DnaK controls the homoeostasis of curli biogenesis at multiple stages to organize the biofilm matrix.