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The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins
DC Field | Value | Language |
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dc.contributor.author | 김종선 | - |
dc.contributor.author | 안근재 | - |
dc.date.accessioned | 2014-12-19T17:37:15Z | - |
dc.date.available | 2014-12-19T17:37:15Z | - |
dc.date.issued | 2012 | - |
dc.identifier.issn | 0887-3585 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/91752 | - |
dc.description.abstract | α-Synuclein is the principal component of the Lewy body deposits that are characteristic of Parkinson's disease. In vivo, and under physiological conditions in vitro, α-synuclein aggregates to form amyloid fibrils, a process that is likely to be associated with the development of Parkinson's disease. α-Synuclein also possesses chaperone activity to prevent the precipitation of amorphously aggregating target proteins, as demonstrated in vitro. α-Synuclein is an intrinsically disordered (i.e., unstructured) protein of 140 amino acids in length, and therefore studies on its fragments can be correlated directly to the functional role of these regions in the intact protein. In this study, the fragment containing residues 61-140 [α-syn(61-140)] was observed to be highly amyloidogenic and was as effective a chaperone in vitro as the full-length protein, while the N- and C-terminal fragments α-syn(1-60) and α-syn(96-140) had no intrinsic chaperone activity. Interestingly, full-length fibrillar α-synuclein had greater chaperone activity than nonfibrillar α-synuclein. It is concluded that the amyloidogenic NAC region (residues 61-95) contains the chaperone-binding site which is optimized for target protein binding as a result of its β-sheet formation and/or ordered aggregation by α-synuclein. On the other hand, the first 60 residues of α-synuclein modulate the protein's chaperone-active site, while at the same time protecting α-synuclein from fibrillation. On its own, however, this fragment [α-syn(1-60)] had a tendency to aggregate amorphously. As a result of this study, the functional roles of the various regions of α-synuclein in its chaperone activity have been delineated. | - |
dc.description.statementOfResponsibility | open | - |
dc.relation.isPartOf | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Amyloid/chemistry | - |
dc.subject.MESH | Amyloid/genetics | - |
dc.subject.MESH | Amyloid/metabolism | - |
dc.subject.MESH | Binding Sites | - |
dc.subject.MESH | Circular Dichroism | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Light | - |
dc.subject.MESH | Molecular Chaperones/metabolism | - |
dc.subject.MESH | Peptide Fragments/chemistry | - |
dc.subject.MESH | Peptide Fragments/genetics | - |
dc.subject.MESH | Peptide Fragments/metabolism* | - |
dc.subject.MESH | Protein Interaction Mapping/methods* | - |
dc.subject.MESH | Recombinant Proteins/chemistry | - |
dc.subject.MESH | Recombinant Proteins/genetics | - |
dc.subject.MESH | Recombinant Proteins/metabolism | - |
dc.subject.MESH | Scattering, Radiation | - |
dc.subject.MESH | Sequence Deletion | - |
dc.subject.MESH | alpha-Synuclein/chemistry | - |
dc.subject.MESH | alpha-Synuclein/genetics | - |
dc.subject.MESH | alpha-Synuclein/metabolism* | - |
dc.title | The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Dermatology (피부과학) | - |
dc.contributor.googleauthor | Agata Rekas | - |
dc.contributor.googleauthor | Keun Jae Ahn | - |
dc.contributor.googleauthor | Jongsun Kim | - |
dc.contributor.googleauthor | John A. Carver | - |
dc.identifier.doi | 10.1002/prot.24028 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A00921 | - |
dc.contributor.localId | A02222 | - |
dc.relation.journalcode | J02565 | - |
dc.identifier.eissn | 1097-0134 | - |
dc.identifier.pmid | 22274962 | - |
dc.identifier.url | http://onlinelibrary.wiley.com/doi/10.1002/prot.24028/abstract | - |
dc.subject.keyword | Parkinson’s disease | - |
dc.subject.keyword | aggregation | - |
dc.subject.keyword | bindingsite | - |
dc.subject.keyword | amyloid fibril | - |
dc.subject.keyword | thioflavin T | - |
dc.subject.keyword | dynamic light scat-tering | - |
dc.subject.keyword | circular dichroism | - |
dc.contributor.alternativeName | Kim, Jong Sun | - |
dc.contributor.alternativeName | Ahn, Keun Jae | - |
dc.contributor.affiliatedAuthor | Kim, Jong Sun | - |
dc.contributor.affiliatedAuthor | Ahn, Keun Jae | - |
dc.citation.volume | 80 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 1316 | - |
dc.citation.endPage | 1325 | - |
dc.identifier.bibliographicCitation | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, Vol.80(5) : 1316-1325, 2012 | - |
dc.identifier.rimsid | 31170 | - |
dc.type.rims | ART | - |
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