A novel approach is presented that combines pulse metabolic labelling with SILAC and BioID mass spectrometry to temporally resolve protein-protein interactions of a co-chaperone to gain novel insights on how co-chaperone-client interactions may occur over the lifespan of a protein to preserve proteostasis.
J1C-PAL is established as a cell-permeable chemoproteomic tool for mapping protein targets and a surprising link between a co-chaperone mimetic and bacterial metabolism is uncovered.
Brock Nelson, Tania J. Lupoli· ChemBioChem· 0 citations
The results reveal distinct ATP- and ADP-state dimer conformations that coexist in equilibrium, and demonstrate that the Hsc70 dimer population is structurally heterogeneous and depends on nucleotide state and cochaperone interactions.
A. Melikov, Vsevolod Viliuga, Daniel Kavan et al.· Journal of Proteome Research· 0 citations
How the regulatory networking of chaperones by cochaperones, particularly J domain proteins (JDPs; also called Hsp40 or DNAJ proteins), contributes to biocondensate formation and protein disaggregation to maintain proteostasis is discussed.
Gregory L. Blatch, Adrienne L. Edkins· 0 citations
It is shown that short nucleic acids containing Gquadruplex (G4) structure can also catalyze protein folding and uncovers a previously underappreciated role for nucleic acid in proteostasis and offers a new strategy for studying nucleic acid structure-function relationship at residue level.
Charge detection mass spectrometry (CDMS) is applied to directly measure the masses of individual DegP ions, resolving the complete oligomeric distribution in the absence and presence of four clients of increasing size and further establishes CDMS as a powerful single-molecule tool for dissecting heterogeneous protein...
Kent R. Vosper, Aizaz Humayun, Matthew S. McPartlan et al.· bioRxiv· 0 citations
Genetic code expansion is used to introduce a photo-crosslinkable unnatural amino acid into the yeast 26S proteasome and capture cellular protein substrates as they translocate through the proteasomal ATPase motor, representing an exciting avenue for probing the landscape of proteasomal substrates and its changes in re...
S. Restrepo, Andreas Martin· bioRxiv· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.