Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis.

ABSTRACT: The canonical function of small heat-shock proteins (sHSPs) is to interact with proteins destabilized under conditions of cellular stress. While the breadth of interactions made by many sHSPs is well-known, there is currently little knowledge about what structural features of the interactors form the basis for their recognition. Here, we have identified 83 in vivo interactors of the sole sHSP in the cyanobacterium Synechocystis sp. PCC 6803, HSP16.6, reflective of stable associations with soluble proteins made under heat-shock conditions. By performing bioinformatic analyses on these interactors, we identify primary and secondary structural elements that are enriched relative to expectations from the cyanobacterial genome. In addition, by examining the Synechocystis interactors and compari

SUBMITTER: Marklund EG 

PROVIDER: S-EPMC6045555 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature