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

Cell Stress & Chaperones
Erik G MarklundElizabeth Vierling

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 comparing them with those identified to bind sHSPs in other prokaryotes, we show that sHSPs associate with specific proteins and biological processes. Our data are therefore consistent with a picture of sHSPs being broadly specific molecular chaperones that act to protect multiple cellular pathways.

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Citations

Nov 6, 2018·The Journal of Biological Chemistry·Martin HaslbeckJohannes Buchner
Jan 9, 2019·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Hajer Salem MalitanThomas H MacRae

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Methods Mentioned

BETA
immunoprecipitation
pull-downs
pull-down
electrophoresis
protein-folding
protein folding

Software Mentioned

regexp
EMBOSS
SEQUEST
DTASelect
PANTHER

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