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10.1016/j.tim.2015.07.010

http://scihub22266oqcxt.onion/10.1016/j.tim.2015.07.010
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C4636965!4636965!26439293
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suck abstract from ncbi


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pmid26439293      Trends+Microbiol 2015 ; 23 (11): 693-706
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  • Bacterial amyloid formation: structural insights into curli biogensis #MMPMID26439293
  • Van Gerven N; Klein R; Hultgren S; Remaut H
  • Trends Microbiol 2015[Nov]; 23 (11): 693-706 PMID26439293show ga
  • Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multi-component secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the buildup of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight in the curli assembly pathway will provide tools for new biotechnological applications, and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation.
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