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한빛사논문
한빛사논문
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Karolinska Institutet, 현 University of Michigan
Proc. Natl. Acad. Sci. USA, Published online before print December 20, 2017 | doi: 10.1073/pnas.1712051115
Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
Changhan Leea,1, Kamila B. Frankeb,2, Shady Mansour Kamala,c,2, Hyunhee Kima,1,2, Heinrich Lunsdorfd, Jasmin Jagerb, Manfred Nimtze, Janja Trčekf, Lothar Jansche, Bernd Bukaub, Axel Mogkb,3, and Ute Romlinga,3
aDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, 17177, Sweden;
aDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, 17177, Sweden;
bCenter for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ?ZMBH Alliance, Heidelberg, 69120, Germany;
cDepartment of Microbiology and Immunology, Faculty of Pharmaceutical Sciences & Pharmaceutical Industries, Future University in Egypt, Cairo, 11835, Egypt;
dCentral Facility for Microscopy, The Helmholtz Centre for Infection Research, Braunschweig, 38124, Germany;
eCellular Proteomics, The Helmholtz Centre for Infection Research, Braunschweig, 38124, Germany;
fFaculty of Natural Sciences and Mathematics, Department of Biology, University of Maribor, Maribor, 2000, Slovenia
1Present address: Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
2K.B.F., S.M.K., and H.K. contributed equally to this work.
3To whom correspondence may be addressed.
Abstract
AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species Pseudomonas aeruginosa and subsequently abundant P. aeruginosa clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of P. aeruginosa primarily in stationary phase and boosts heat resistance 100-fold when expressed in Escherichia coli. This qualifies ClpG as a potential persistence and virulence factor in P. aeruginosa.
protein disaggregation, AAA+ protein, heat tolerance, mobile genetic element, Hsp100
protein disaggregation, AAA+ protein, heat tolerance, mobile genetic element, Hsp100
논문정보
- Research article
- 2017년 12월 (BRIC 등록일 2018-01-02)
- 국외 연구진
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