BACKGROUND: The formation of protein inclusions is connected to the onset of many @entity1 diseases. @entity1 RNA binding proteins containing intrinsically disordered regions with an @entity3689 composition resembling those of @entity375 prion domains, like @entity529 or FUS, are being found to aggregate in different @entity179 . The structure of the intracellular inclusions formed by these proteins is still unclear and whether these deposits have an @entity10543 nature or not is a matter of debate. Recently, the aggregation of @entity529 has been modelled in bacteria, showing that @entity529 inclusion bodies (IBs) are amorphous but intrinsically @entity2359 . This observation raises the question of whether it is indeed the lack of an ordered structure in these @entity1 prion-like protein aggregates the underlying cause of their @entity137 in different pathological states. RESULTS: Here we characterize the IBs formed by the @entity1 prion-like RNA-processing protein @entity24062 . @entity24062 is linked to the development of @entity17325 1G and shares domain architecture with @entity529 . We show that @entity24062 IBs display characteristic @entity10543 , since these aggregates bind to @entity10543 dyes in vitro and inside the cell, they are enriched in intermolecular b-sheet conformation and contain inner @entity10543 -like fibrillar structure. In addition, despite their ordered structure, @entity24062 IBs are highly @entity2359 . CONCLUSIONS: Our results suggest that at least some of the disorders caused by the aggregation of @entity1 prion-like proteins would rely on the formation of classical @entity10543 assemblies rather than being caused by amorphous aggregates. They also illustrate the power of microbial cell factories to model @entity1423 .

The prion-like RNA-processing protein XXXX forms inherently toxic @entity10543 -like inclusion bodies in bacteria.

@entity1 :: ('9606', 'Species') :: ['human', 'Human'] @entity137 :: ('MESH:D064420', 'Disease') :: ['toxicity'] @entity1423 :: ('MESH:D001791', 'Disease') :: ['amyloid aggregation'] @entity24062 :: ('9987', 'Gene') :: ['HNRPDL'] @entity10543 :: ('MESH:D017772', 'Disease') :: ['amyloid', 'amyloid hallmarks'] @entity179 :: ('MESH:D019636', 'Disease') :: ['neurodegenerative disorders'] @entity17325 :: ('MESH:D049288', 'Disease') :: ['limb-girdle muscular dystrophy'] @entity3689 :: ('D000596', 'Chemical') :: ['amino acid'] @entity375 :: ('4932', 'Species') :: ['yeast'] @entity529 :: ('23435', 'Gene') :: ['TDP-43'] @entity2359 :: ('MESH:D020258', 'Disease') :: ['neurotoxic']
@entity24062 :: (9987,Gene) :: ['HNRPDL']
