Publications by authors named "Chihaya Sakuhana"
The chaperonin GroEL assists protein folding in the presence of ATP and magnesium through substrate protein capsulation in combination with the cofactor GroES. Recent studies have revealed the details of folding cycles of GroEL from Escherichia coli, yet little is known about the GroEL-assisted protein folding mechanisms in other bacterial species. Using three model enzyme assays, we have found that GroEL1 from Chlamydophila pneumoniae, an obligate human pathogen, has a broader selectivity for nucleotides in the refolding reaction.
View Article and Find Full Text PDFArticle Synopsis
- Chaperonin GroEL, with the help of ATP and magnesium, plays a crucial role in assisting protein folding.
- Recent research indicates that other divalent cations, like manganese, can also affect GroEL's folding function, but the specific mechanisms are not well understood.
- The study found that while manganese supports protein refolding, zinc inhibits it, and cobalt and nickel allow stable GroEL complexes but hinder the release of the refolded protein METF.