Global unfolding of a substrate protein by the Hsp100 chaperone ClpA

Article Abstract:

It has been shown that, in the presence of ATP, the bacterial protein ClpA, which belongs to the Hsp100 chaperone family, mediates the unfolding of proteins bound after recognition of specific terminal amino-acid sequences. In connection with ClpP protease, the destabilized structures are committed to translocation from the cavity of ClpA into the hydrolytic cavity of the protease, where they are degraded. When associated ClpP is not present, substrate proteins pass from ClpA into solution, where spontaneous refolding or binding may take place.

---

Where do the electrons go?

Article Abstract:

New research has produced strong experimental evidence that, in bacteria, oxidative protein folding is coupled to the electron-transport chain. It was found that, in vitro, pure DsbB catalyzes the oxidation of DsbA by ubiquinone derivatives very efficiently. This research has also identified the pathway of electron flow that guarantees the formation of disulphide bonds in the absence of oxygen.

---

Similar abstracts:

• Abstracts: Identification of in vivo substrates of the chaperonin GroEL. A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form
• Abstracts: Influence of CO2 emission rates on the stability of the thermohaline circulation. Models change their tune
• Abstracts: Enzymatic capture of an extrahelical thymine in the search for uracil in DNA. Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C
• Abstracts: A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Spindle saga

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.