The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP

Frontiers in Molecular Biosciences
Christopher J LaBreckJodi L Camberg

Abstract

ClpX is a member of the Clp/Hsp100 family of ATP-dependent chaperones and partners with ClpP, a compartmentalized protease, to degrade protein substrates bearing specific recognition signals. ClpX targets specific proteins for degradation directly or with substrate-specific adaptor proteins. Native substrates of ClpXP include proteins that form large oligomeric assemblies, such as MuA, FtsZ, and Dps inEscherichia coli. To remodel large oligomeric substrates, ClpX utilizes multivalent targeting strategies and discriminates between assembled and unassembled substrate conformations. Although ClpX and ClpP are known to associate with protein aggregates inE. coli, a potential role for ClpXP in disaggregation remains poorly characterized. Here, we discuss strategies utilized by ClpX to recognize native and non-native protein aggregates and the mechanisms by which ClpX alone, and with ClpP, remodels the conformations of various aggregates. We show that ClpX promotes the disassembly and reactivation of aggregated Gfp-ssrA through specific substrate remodeling. In the presence of ClpP, ClpX promotes disassembly and degradation of aggregated substrates bearing specific ClpX recognition signals, including heat-aggregated Gfp-ssrA, as well...Continue Reading

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Citations

Sep 20, 2018·Molecular Microbiology·Jaana MännikJaan Männik
Jan 12, 2019·Pharmaceutical Patent Analyst·Hermann Am Mucke
Feb 13, 2019·Cold Spring Harbor Perspectives in Biology·James Shorter, Daniel R Southworth
Oct 22, 2019·FEMS Microbiology Reviews·Frederic D SchrammKristina Jonas
Jan 31, 2020·The FEBS Journal·Sonia HuecasJosé M Andreu
Apr 18, 2020·Applied Microbiology and Biotechnology·Mingzhu HuangXuelan Chen
Feb 26, 2019·Microbial Biotechnology·Grégory BoëlAntoine Danchin
Dec 9, 2020·The Journal of Biological Chemistry·Christopher J LaBreckJodi L Camberg

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Methods Mentioned

BETA
protein folding
environmental stress
thermal stress
dynamic light scattering
light scattering
GTPase

Software Mentioned

GraphPad Prism

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