Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies

FEMS Yeast Research
Rupam GhoshKendra K Frederick

Abstract

Yeast prions are self-templating protein-based mechanisms of inheritance whose conformational changes lead to the acquisition of diverse new phenotypes. The best studied of these is the prion domain (NM) of Sup35, which forms an amyloid that can adopt several distinct conformations (strains) that confer distinct phenotypes when introduced into cells that do not carry the prion. Here, we investigate the structure of NM fibrils templated into the prion conformation with cellular lysates. Our electron microscopy studies reveal that NM fibrils that confer either a strong or a weak prion phenotype are both mixtures of thin and thick fibrils that result from differences in packing of the M domain. Strong NM fibrils have more thin fibrils and weak NM fibrils have more thick fibrils. Interestingly, both mass per length and solid state NMR reveal that the thin and thick fibrils have different underlying molecular structures in the prion strain variants that do not interconvert.

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Citations

Dec 27, 2019·Prion·Vitaly V KushnirovAlexander I Alexandrov
Mar 29, 2020·BMC Biology·Giulio ChiesaAhmad S Khalil
May 31, 2019·International Journal of Molecular Sciences·Alexander A DergalevVitaly V Kushnirov
Nov 11, 2020·Proceedings of the National Academy of Sciences of the United States of America·Yiling XiaoBengt Nordén
Jul 26, 2019·Seminars in Cell & Developmental Biology·Johannes Manjrekar, Hiral Shah
Jun 3, 2020·Langmuir : the ACS Journal of Surfaces and Colloids·Michael J LucasBenjamin K Keitz

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Methods Mentioned

BETA
transmission electron microscopy
NMR
protein folding

Software Mentioned

GeneScript
PCMass32
PCMass
STEM

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