KLR-70: A Novel Cationic Inhibitor of the Bacterial Hsp70 Chaperone.

ABSTRACT: The heat-shock factor Hsp70 and other molecular chaperones play a central role in nascent protein folding. Elucidating the task performed by individual chaperones within the complex cellular milieu, however, has been challenging. One strategy for addressing this goal has been to monitor protein biogenesis in the absence and presence of inhibitors of a specific chaperone, followed by analysis of folding outcomes under both conditions. In this way, the role of the chaperone of interest can be discerned. However, development of chaperone inhibitors, including well-known proline-rich antimicrobial peptides, has been fraught with undesirable side effects, including decreased protein expression yields. Here, we introduce KLR-70, a rationally designed cationic inhibitor of the Escherichia coli

SUBMITTER: Dalphin MD 

PROVIDER: S-EPMC8322834 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature