Your browser doesn't support javascript.
loading
Huntingtin Polyglutamine-Dependent Protein Aggregation in Reconstituted Cells.
Machida, Kodai; Kanzawa, Kuru; Shigeta, Tomoaki; Yamamoto, Yuki; Tsumoto, Kanta; Imataka, Hiroaki.
Affiliation
  • Machida K; Department of Applied Chemistry, Graduate School of Engineering, University of Hyogo , Himeji 671-2201, Japan.
  • Kanzawa K; RIKEN Center for Life Science Technologies , Yokohama 230-0045, Japan.
  • Shigeta T; Department of Applied Chemistry, Graduate School of Engineering, University of Hyogo , Himeji 671-2201, Japan.
  • Yamamoto Y; Department of Applied Chemistry, Graduate School of Engineering, University of Hyogo , Himeji 671-2201, Japan.
  • Tsumoto K; Department of Applied Chemistry, Graduate School of Engineering, University of Hyogo , Himeji 671-2201, Japan.
  • Imataka H; Division of Chemistry for Materials, Graduate School of Engineering, Mie University , Tsu 514-8507, Japan.
ACS Synth Biol ; 7(2): 377-383, 2018 02 16.
Article in En | MEDLINE | ID: mdl-29232946
One of the aims of synthetic biology is bottom-up construction of reconstituted human cells for medical uses. To that end, we generated giant unilamellar vesicles (GUVs) that contained a HeLa cell extract, which comprises a cell-free protein synthesis (CFPS) system. Then we expressed Huntingtin protein fragments that contained polyglutamine (polyQ) sequences (Htt-polyQ), a hallmark of Huntington's disease. That system produced polyQ-dependent protein aggregates, as previously demonstrated in living cells. We next simplified the system by generating GUVs that contained purified human factors, which reconstituted a CFPS system. Htt-polyQ fragments expressed in these GUVs also formed protein aggregates. Moreover, an N-terminal deletion mutant, which had failed to form protein aggregates in living cells, also failed to form protein aggregates in the reconstituted GUVs. Thus, the GUV systems that encapsulated a human CFPS system could serve as reconstituted cells for studying neurological diseases.
Subject(s)
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Unilamellar Liposomes / Protein Aggregation, Pathological / Huntingtin Protein / Mutation Limits: Humans Language: En Journal: ACS Synth Biol Year: 2018 Document type: Article Affiliation country: Japan Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Unilamellar Liposomes / Protein Aggregation, Pathological / Huntingtin Protein / Mutation Limits: Humans Language: En Journal: ACS Synth Biol Year: 2018 Document type: Article Affiliation country: Japan Country of publication: United States