MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated by coiled-coil interactions and that MED15CC aggreg...

Full description

Bibliographic Details
Main Authors: Cristina Batlle, Isabel Calvo, Valentin Iglesias, Cian J. Lynch, Marcos Gil-Garcia, Manuel Serrano, Salvador Ventura
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-01930-8
Description
Summary:Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated by coiled-coil interactions and that MED15CC aggregates into amyloid fibrils.
ISSN:2399-3642

Similar Items