Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.

ABSTRACT: The 70-kD heat shock protein (Hsp70) chaperone system is a central hub of the proteostasis network that helps maintain protein homeostasis in all organisms. The recruitment of Hsp70 to perform different and specific cellular functions is regulated by the J-domain protein (JDP) co-chaperone family carrying the small namesake J-domain, required to interact and drive the ATPase cycle of Hsp70s. Besides the J-domain, prokaryotic and eukaryotic JDPs display a staggering diversity in domain architecture, function, and cellular localization. Very little is known about the overall JDP family, despite their essential role in cellular proteostasis, development, and its link to a broad range of human diseases. In this work, we leverage the exponentially increasing number of JDP gene sequences identif

SUBMITTER: Malinverni D 

PROVIDER: S-EPMC10410713 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature