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Proc Natl Acad Sci U S A. 2015 Jan 6;112(1):250-5. doi: 10.1073/pnas.1417419112. Epub 2014 Dec 23.

Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellation.

Author information

1
Department of Biology, Indiana University, Bloomington, IN 47405; and.
2
Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA 01003.
3
Department of Biology, Indiana University, Bloomington, IN 47405; and dbkearns@indiana.edu.

Abstract

The Lon AAA+ protease is a highly conserved intracellular protease that is considered an anticancer target in eukaryotic cells and a crucial virulence regulator in bacteria. Lon degrades both damaged, misfolded proteins and specific native regulators, but how Lon discriminates among a large pool of candidate targets remains unclear. Here we report that Bacillus subtilis LonA specifically degrades the master regulator of flagellar biosynthesis SwrA governed by the adaptor protein swarming motility inhibitor A (SmiA). SmiA-dependent LonA proteolysis is abrogated upon microbe-substrate contact causing SwrA protein levels to increase and elevate flagellar density above a critical threshold for swarming motility atop solid surfaces. Surface contact-dependent cellular differentiation in bacteria is rapid, and regulated proteolysis may be a general mechanism of transducing surface stimuli.

KEYWORDS:

LonA; SwrA; adaptor; flagella; regulatory proteolysis

PMID:
25538299
PMCID:
PMC4291670
DOI:
10.1073/pnas.1417419112
[Indexed for MEDLINE]
Free PMC Article

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