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Bacterial Inclusion Bodies Contain Amyloid-Like Structure.doc

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Bacterial Inclusion Bodies Contain Amyloid-Like Structure

o PL SBIOLOGY BacterialInclusionBodiesContain Amyloid-LikeStructure Lei Wang1,Samir K. Maji1,Michael R.Sawaya2,3,David Eisenberg2,3,Roland Riek1,4* 1StructuralBiologyLaboratory,TheSalkInstitute,LaJolla,California,UnitedStatesofAmerica,2HowardHughesMedicalInstitute,UniversityofCalifornia,LosAngeles,Los Angeles,California,UnitedStatesofAmerica,3UniversityofCalifornia,LosAngeles–DepartmentofEnergy(UCLA-DOE)InstituteforGenomicsandProteomics,Universityof California,LosAngeles,LosAngeles,California,UnitedStatesofAmerica,4LaboratoryofPhysicalChemistry,SwissFederalInstituteofTechnology(ETH),Zurich,Switzerland Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities.Suchaggregatesaregenerallyclassifiedasamorphous,lackinganylong-rangeorder,orhighlyorderedfibrils. Proteinfibrilscanbecomposedofnativeglobularmolecules,suchasthehemoglobinmoleculesinsickle-cellfibrils,or can be reorganized b-sheet–rich aggregates, termed amyloid-like fibrils. Amyloid fibrils are associated with several pathological conditions in humans, including Alzheimer disease and diabetes type II. We studied the structure of bacterialinclusionbodies,whichhavebeenbelievedtobelongtotheamorphousclassofaggregates.Wedemonstrate thatallthreeinvivo-derivedinclusionbodiesstudiedareamyloid-likeandcomprisedofamino-acidsequence-specific cross-b structure. These findings suggest that inclusion bodies are structured, that amyloid formation is an omnipresentprocessbothineukaryotesandprokaryotes,andthataminoacidsequencesevolvetoavoidtheamyloid conformation. Citation:WangL,MajiSK,SawayaMR,EisenbergD,RiekR(2008)Bacterialinclusionbodiescontainamyloid-likestructure.PLoSBiol6(8):e195.doi:10.1371/journal.pbio. 0060195 studied are amyloid-like, comprising amino acid sequence- speci?ccross-bstructure. Introduction Theconversionofpeptidesandproteinsintoaggregatesis associated with several dozen pathological conditions in humans, including Alzheimer disease, Parkins