Molecular machines that facilitate bacterial outer membrane protein biogenesis

MT Doyle, HD Bernstein - Annual Review of Biochemistry, 2024 - annualreviews.org
Almost all outer membrane proteins (OMPs) in Gram-negative bacteria contain a β-barrel
domain that spans the outer membrane (OM). To reach the OM, OMPs must be translocated …

Periplasmic chaperones: outer membrane biogenesis and envelope stress

AN Combs, TJ Silhavy - Annual Review of Microbiology, 2024 - annualreviews.org
Envelope biogenesis and homeostasis in gram-negative bacteria are exceptionally intricate
processes that require a multitude of periplasmic chaperones to ensure cellular survival …

Regulation of α-synuclein by chaperones in mammalian cells

BM Burmann, JA Gerez, I Matečko-Burmann… - Nature, 2020 - nature.com
Neurodegeneration in patients with Parkinson's disease is correlated with the occurrence of
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function

TR Alderson, LE Kay - Cell, 2021 - cell.com
Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

Outer membrane protein biogenesis in Gram-negative bacteria

SE Rollauer, MA Sooreshjani… - … Transactions of the …, 2015 - royalsocietypublishing.org
Gram-negative bacteria contain a double membrane which serves for both protection and for
providing nutrients for viability. The outermost of these membranes is called the outer …

Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

MG Iadanza, AJ Higgins, B Schiffrin… - Nature …, 2016 - nature.com
The β-barrel assembly machinery (BAM) is a∼ 203 kDa complex of five proteins (BamA–E),
which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel …

Structural basis for protein antiaggregation activity of the trigger factor chaperone

T Saio, X Guan, P Rossi, A Economou, CG Kalodimos - Science, 2014 - science.org
Introduction Molecular chaperones prevent aggregation and misfolding of proteins in the
cellular environment and are thus central to maintaining protein homeostasis. Molecular …

Structural basis for client recognition and activity of Hsp40 chaperones

Y Jiang, P Rossi, CG Kalodimos - Science, 2019 - science.org
Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes
including protein synthesis, membrane translocation, and folding. We used nuclear …

Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon

F Lauber, JC Deme, X Liu, A Kjær, HL Miller… - Nature …, 2024 - nature.com
Secretion systems are protein export machines that enable bacteria to exploit their
environment through the release of protein effectors. The Type 9 Secretion System (T9SS) is …

Structural basis for the antifolding activity of a molecular chaperone

C Huang, P Rossi, T Saio, CG Kalodimos - Nature, 2016 - nature.com
Molecular chaperones act on non-native proteins in the cell to prevent their aggregation,
premature folding or misfolding. Different chaperones often exert distinct effects, such as …