| http://purl.uniprot.org/citations/24778935 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24778935 | http://www.w3.org/2000/01/rdf-schema#comment | "The centriole is a conserved microtubule-based organelle essential for both centrosome formation and cilium biogenesis. It has a unique 9-fold symmetry and its assembly is governed by at least five component proteins (SPD-2, ZYG-1, SAS-5, SAS-6 and SAS-4), which are recruited in a hierarchical order. Recently published structural studies of the SAS-6 N-terminal domain have greatly advanced our understanding of the mechanisms of centriole assembly. However, it remains unclear how the weak interaction between the SAS-6 N-terminal head groups could drive the assembly of a closed ring-like structure, and what determines the stacking of multiple rings on top one another in centriole duplication. We recently reported that SAS-5 binds specifically to a very narrow region of the SAS-6 central coiled coil through its C-terminal domain (CTD, residues 391-404). Here, we further demonstrate by both static light scattering and small angle X-ray scattering that the SAS-5 N-terminal domain (NTD, residues 1-260) forms a tetramer. Specifically, we found that the tetramer is formed by SAS-5 residues 82-260, whereas residues 1-81 are intrinsically disordered. Taking these results together, we propose a working model for SAS-5-mediated assembly of the multi-layered central tube structure."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.org/dc/terms/identifier | "doi:10.4161/worm.25214"xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/author | "Dong G."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/author | "Qiao R."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/author | "Lesigang J."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/author | "Shimanovskaya E."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/name | "Worm"xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/pages | "e25214"xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/title | "The SAS-5 N-terminal domain is a tetramer, with implications for centriole assembly in C. elegans."xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://purl.uniprot.org/core/volume | "2"xsd:string |
| http://purl.uniprot.org/citations/24778935 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24778935 |
| http://purl.uniprot.org/citations/24778935 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24778935 |
| http://purl.uniprot.org/uniprot/#_Q20010-mappedCitation-24778935 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24778935 |
| http://purl.uniprot.org/uniprot/Q20010 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24778935 |