Publications by authors named "Danielle M Johnston"
Article Synopsis
- ClpB and yeast Hsp104 are related molecular chaperones that help proteins regain their function after being stressed or aggregated, and they are part of the AAA+ ATPase family.
- They work alongside the DnaK and Hsp70 chaperone systems to tackle protein aggregates, which are important for thermotolerance and prion propagation in yeast.
- The study identified that the specific substrate preferences of ClpB and Hsp104, even without the assistance of DnaK and Hsp70, are influenced by a specific region called nucleotide binding domain-1.
Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases. Hsp104 and ClpB collaborate with the Hsp70 and DnaK chaperone systems, respectively, to retrieve and reactivate stress-denatured proteins from aggregates. The action of Hsp104 and ClpB in promoting cell survival following heat stress is species-specific: Hsp104 cannot function in bacteria and ClpB cannot act in yeast.
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