A prionogenic peptide derived from Sup35 can force the whole GST fusion protein to show amyloid characteristics.
A prion determining 7-mer peptide derived from Sup35 was fused to glutathione S transferase (GST). The fusion protein was successfully overexpressed in Escherichia coli, and purified by employing affinity chromatography. Upon incubation, it showed substantial aggregation suggesting the formation of amyloid-like fibrils. Congo Red binding strongly suggested that the fusion protein formed amyloid-like fibrils. By considering the steric hindrance of GST, the beta-sheet formation should be in the anti-parallel fashion.
Chae
Young Kee
YK
Department of Applied Chemistry and Recombinant Protein Expression Center (RPEC), Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul, 143-747, Korea.
Cho
Kyoung Suk
KS
Chun
Woochun
W
D004396:Coloring Agents / Q000378:metabolism; D003224:Congo Red / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D017930:Genes, Reporter; D010454:Peptide Termination Factors; D010455:Peptides / Q000235:genetics / Q000378:metabolism*; D011328:Prions / Q000378:metabolism*; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D004396:Coloring Agents; D005656:Fungal Proteins; D010454:Peptide Termination Factors; D010455:Peptides; D011328:Prions; D011993:Recombinant Fusion Proteins; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D003224:Congo Red