The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines
ATPases associated with diverse cellular activities (AAA+ proteins) are a superfamily of
proteins found throughout all domains of life. The hallmark of this family is a conserved …
proteins found throughout all domains of life. The hallmark of this family is a conserved …
The molecular principles governing the activity and functional diversity of AAA+ proteins
ATPases associated with diverse cellular activities (AAA+ proteins) are macromolecular
machines that convert the chemical energy contained in ATP molecules into powerful …
machines that convert the chemical energy contained in ATP molecules into powerful …
Bottom-up fabrication of a proteasome–nanopore that unravels and processes single proteins
S Zhang, G Huang, RCA Versloot, BMH Bruininks… - Nature …, 2021 - nature.com
The precise assembly and engineering of molecular machines capable of handling
biomolecules play crucial roles in most single-molecule methods. In this work we use …
biomolecules play crucial roles in most single-molecule methods. In this work we use …
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and
translocates specific protein substrates into the degradation chamber of ClpP. We present …
translocates specific protein substrates into the degradation chamber of ClpP. We present …
Structure, dynamics and function of the 26S proteasome
Y Mao - Macromolecular protein complexes III: structure and …, 2021 - Springer
The 26S proteasome is the most complex ATP-dependent protease machinery, of~ 2.5 MDa
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …
A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair
of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently …
of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently …
Proteasome in action: substrate degradation by the 26S proteasome
I Sahu, MH Glickman - Biochemical Society Transactions, 2021 - portlandpress.com
Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S
proteasome. Additionally, a disordered segment on the substrate—either intrinsic or induced …
proteasome. Additionally, a disordered segment on the substrate—either intrinsic or induced …
The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges
GR Tundo, D Sbardella, AM Santoro, A Coletta… - Pharmacology & …, 2020 - Elsevier
Abstract Ubiquitin Proteasome System (UPS) is an adaptable and finely tuned system that
sustains proteostasis network under a large variety of physiopathological conditions. Its …
sustains proteostasis network under a large variety of physiopathological conditions. Its …
Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules
MF Mabanglo, WA Houry - Journal of Biological Chemistry, 2022 - ASBMB
ClpP is a highly conserved serine protease that is a critical enzyme in maintaining protein
homeostasis and is an important drug target in pathogenic bacteria and various cancers. In …
homeostasis and is an important drug target in pathogenic bacteria and various cancers. In …
[HTML][HTML] The pre-synaptic fusion machinery
AT Brunger, UB Choi, Y Lai, J Leitz, KI White… - Current opinion in …, 2019 - Elsevier
Highlights•Structure of a pre-fusion synaptic complex.•Regulated assembly of SNARE
complex.•Mechanism of NSF-mediated disassembly of the SNARE complex.Here, we review …
complex.•Mechanism of NSF-mediated disassembly of the SNARE complex.Here, we review …