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The non-canonical small heat shock protein from C. elegans is a molecular aggregase

ABSTRACT: Physiological interaction partners of the small heat shock protein HSP-17 from C. elegans were to be identified in the context of a study on the function of this non-canonical small heat shock protein in vivo and in vitro. An immunoprecipitation with an antibody raised against HSP-17 was performed on lysates of wild type C. elegans, followed by MS analysis.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Manuel Iburg

LAB HEAD: Janine Kirstein

PROVIDER: PXD016485 | Pride | 2020-03-23

REPOSITORIES: pride

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	E1_20181010_HS_930_JK_IP_A1.raw	Raw
	E1_20181010_HS_930_JK_IP_A1P.raw	Raw
	E1_20181010_HS_930_JK_IP_A2.raw	Raw
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	E1_20181010_HS_930_JK_IP_B1.raw	Raw

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Publications

The noncanonical small heat shock protein HSP-17 from <i>Caenorhabditis elegans</i> is a selective protein aggregase.

Iburg Manuel M Puchkov Dmytro D Rosas-Brugada Irving U IU Bergemann Linda L Rieprecht Ulrike U Kirstein Janine J

The Journal of biological chemistry 20200130 10

Small heat shock proteins (sHsps) are conserved, ubiquitous members of the proteostasis network. Canonically, they act as "holdases" and buffer unfolded or misfolded proteins against aggregation in an ATP-independent manner. Whereas bacteria and yeast each have only two sHsps in their genomes, this number is higher in metazoan genomes, suggesting a spatiotemporal and functional specialization in higher eukaryotes. Here, using recombinantly expressed and purified proteins, static light-scattering ...[more]

PMID: 32001616

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The human Ewing's Sarcoma oncoprotein EWS-FLI1 causes Ewing's-type tumors in zebrafish

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