Protein folding and aggregation in bacteria.
Proteins might experience many conformational changes and interactions during their lifetimes, from their synthesis at ribosomes to their controlled degradation. Because, in most cases, only folded proteins are functional, protein folding in bacteria is tightly controlled genetically, transcriptionally, and at the protein sequence level. In addition, important cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of functional structures. When these redundant protective strategies are overcome, misfolded polypeptides are recruited into insoluble inclusion bodies. The protein embedded in these intracellular deposits might display different conformations including functional and beta-sheet-rich structures. The latter assemblies are similar to the amyloid fibrils characteristic of several human neurodegenerative diseases. Interestingly, bacteria exploit the same structural principles for functional properties such as adhesion or cytotoxicity. Overall, this review illustrates how prokaryotic organisms might provide the bedrock on which to understand the complexity of protein folding and aggregation in the cell.
Sabate
Raimon
R
Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain.
de Groot
Natalia S
NS
Ventura
Salvador
S
D000682:Amyloid / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism / Q000648:ultrastructure; D007239:Infections / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D012270:Ribosomes / Q000378:metabolism
D000682:Amyloid; D001426:Bacterial Proteins; D006025:Glycosaminoglycans; D018832:Molecular Chaperones