RESUMO

GRASPs are proteins involved in cell processes that seem paradoxical: responsible for shaping the Golgi cisternae and involved in unconventional secretion mechanisms that bypass the Golgi. Despite its physiological relevance, there is still a considerable lack of studies on full-length GRASPs. Our group has previously reported an unexpected behavior of the full-length GRASP from the fungus C. neoformans: its intrinsically-disordered characteristic. Here, we generalize this finding by showing that it is also observed in the GRASP from S. cerevisae (Grh1), which strongly suggests it might be a general property within the GRASP family. Furthermore, Grh1 is also able to form amyloid-like fibrils either upon heating or when submitted to changes in the dielectric constant of its surroundings, a condition that is experienced by the protein when in close contact with membranes of cell compartments, such as the Golgi apparatus. Intrinsic disorder and fibril formation can thus be two structural properties exploited by GRASP during its functional cycle.

Assuntos

Proteínas Amiloidogênicas/química , Proteínas Intrinsicamente Desordenadas/química , Peptídeos/química , Proteínas de Saccharomyces cerevisiae/química , Proteínas de Transporte Vesicular/química , Sequência de Aminoácidos , Amiloide/química , Benzotiazóis/química , Dicroísmo Circular , Vermelho Congo/química , Complexo de Golgi/metabolismo , Proteínas da Matriz do Complexo de Golgi/química , Imagem Óptica , Conformação Proteica em Folha beta , Desnaturação Proteica , Saccharomyces cerevisiae/metabolismo , Solventes/química , Espectrometria de Fluorescência , Temperatura , Rede trans-Golgi/metabolismo