Fundamental characteristics of AAA+ protein family structure and function

JM Miller, EJ Enemark - Archaea, 2016 - Wiley Online Library
Many complex cellular events depend on multiprotein complexes known as molecular
machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to …

AAA+ proteins: one motor, multiple ways to work

JB Lin, J Shorter, AL Lucius - Biochemical Society Transactions, 2022 - portlandpress.com
Numerous ATPases associated with diverse cellular activities (AAA+) proteins form
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …

Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis

KE Lopez, AN Rizo, E Tse, JB Lin, NW Scull… - Nature Structural & …, 2020 - nature.com
The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins
targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and …

Multi-start Evolutionary Nonlinear OpTimizeR (MENOTR): A hybrid parameter optimization toolbox

ZM Ingram, NW Scull, DS Schneider, AL Lucius - Biophysical chemistry, 2021 - Elsevier
Parameter optimization or “data fitting” is a computational process that identifies a set of
parameter values that best describe an experimental data set. Parameter optimization is …

[HTML][HTML] Comparative analysis of the structure and function of AAA+ motors ClpA, ClpB, and Hsp104: Common threads and disparate functions

EC Duran, CL Weaver, AL Lucius - Frontiers in molecular biosciences, 2017 - frontiersin.org
Cellular proteostasis involves not only the expression of proteins in response to
environmental needs, but also the timely repair or removal of damaged or unneeded …

Escherichia coli ClpB is a non-processive polypeptide translocase

T Li, CL Weaver, J Lin, EC Duran, JM Miller… - Biochemical …, 2015 - portlandpress.com
Escherichia coli caseinolytic protease (Clp) B is a hexameric AAA+ [expanded superfamily
of AAA (ATPase associated with various cellular activities)] enzyme that has the unique …

E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP

JM Miller, J Lin, T Li, AL Lucius - Journal of molecular biology, 2013 - Elsevier
There are five known ATP-dependent proteases in Escherichia coli (Lon, ClpAP, ClpXP,
HslUV, and the membrane-associated FtsH) that catalyze the removal of both misfolded and …

[HTML][HTML] Mycobacterium tuberculosis ClpC1 N-Terminal Domain Is Dispensable for Adaptor Protein-Dependent Allosteric Regulation

JD Marsee, A Ridings, T Yu, JM Miller - International journal of molecular …, 2018 - mdpi.com
ClpC1 hexamers couple the energy of ATP hydrolysis to unfold and, subsequently,
translocate specific protein substrates into the associated ClpP protease. Substrate …

Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA

R Galletto, EJ Tomko - Nucleic acids research, 2013 - academic.oup.com
Abstract In Saccharomyces cerevisiae Pif1 participates in a wide variety of DNA metabolic
pathways both in the nucleus and in mitochondria. The ability of Pif1 to hydrolyse ATP and …

[HTML][HTML] Hsp104 and potentiated variants can operate as distinct nonprocessive translocases

CL Durie, JB Lin, NW Scull, KL Mack, ME Jackrel… - Biophysical …, 2019 - cell.com
Heat shock protein (Hsp) 104 is a hexameric ATPases associated with diverse cellular
activities motor protein that enables cells to survive extreme stress. Hsp104 couples the …