The complex role of the N-terminus and acidic residues of HdeA as pH-dependent switches in its chaperone function.

ABSTRACT: HdeA is a small acid-stress chaperone protein found in the periplasm of several pathogenic gram-negative bacteria. In neutral pH environments HdeA is an inactive folded homodimer but when exposed to strong acidic environments it partially unfolds and, once activated, binds to other periplasmic proteins, protecting them from irreversible aggregation. Here we use a combination of hydrogen/deuterium exchange NMR experiments and constant pH molecular dynamics simulations to elucidate the role of HdeA's N-terminus in its activation mechanism. Previous work indicates that the N-terminus is flexible and unprotected at high pH while exhibiting interactions with some HdeA client binding site residues. It, however, becomes partially solvent-protected at pH 2.6 - 2.8 and then loses protection again a

SUBMITTER: Pacheco S 

PROVIDER: S-EPMC8276670 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature