Unknown

Dataset Information

0

Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.


ABSTRACT: We have studied the interaction of the prototypical chaperonin GroEL with the prion domain of the Het-s protein using solution and solid-state NMR, electron and atomic force microscopies, and EPR. While GroEL accelerates Het-s protofibril formation by several orders of magnitude, the rate of appearance of fibrils is reduced. GroEL remains bound to Het-s throughout the aggregation process and densely decorates the fibrils at a regular spacing of ?200 Å. GroEL binds to the Het-s fibrils via its apical domain located at the top of the large open ring. Thus, apo GroEL and bullet-shaped GroEL/GroES complexes in which only a single ring is capped by GroES interact with the Het-s fibrils; no evidence is seen for any interaction with football-shaped GroEL/GroES complexes in which both rings are capped by GroES. EPR spectroscopy shows that rotational motion of a nitroxide spin label, placed at the N-terminal end of the first ?-strand of Het-s fibrils, is significantly reduced in both Het-s/GroEL aggregates and Het-s fibrils, but virtually completely eliminated in Het-s/GroEL fibrils, suggesting that in the latter, GroEL may come into close proximity to the nitroxide label. Solid-state NMR measurements indicate that GroEL binds to the mobile regions of the Het-s fibril comprising the N-terminal tail and a loop connecting ?-strands 4 and 5, consistent with interactions involving GroEL binding consensus sequences located therein.

SUBMITTER: Walti MA 

PROVIDER: S-EPMC5576843 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.

Wälti Marielle A MA   Schmidt Thomas T   Murray Dylan T DT   Wang Huaibin H   Hinshaw Jenny E JE   Clore G Marius GM  

Proceedings of the National Academy of Sciences of the United States of America 20170807 34


We have studied the interaction of the prototypical chaperonin GroEL with the prion domain of the Het-s protein using solution and solid-state NMR, electron and atomic force microscopies, and EPR. While GroEL accelerates Het-s protofibril formation by several orders of magnitude, the rate of appearance of fibrils is reduced. GroEL remains bound to Het-s throughout the aggregation process and densely decorates the fibrils at a regular spacing of ∼200 Å. GroEL binds to the Het-s fibrils via its ap  ...[more]

Similar Datasets

| S-EPMC356944 | biostudies-literature
| S-EPMC4156775 | biostudies-literature
| S-EPMC5899736 | biostudies-literature
| S-EPMC7067779 | biostudies-literature
| S-EPMC4071350 | biostudies-literature
| S-EPMC1885994 | biostudies-literature
| S-EPMC7341905 | biostudies-literature
| S-EPMC4231684 | biostudies-literature
| S-EPMC7440923 | biostudies-literature
| S-EPMC1188259 | biostudies-literature