Redefining Molecular Chaperones as Chaotropes

Molecular Chaperones and Co-chaperones as Therapeutic Targets for Cancer

Cancer is a devastating disease that has affected millions of people, consumed tremendous efforts in the treatment/care and is incurable. Statistics from www.seer.cancer.gov show 14,140,254 people were living with cancer in 2013 in US with 1,685,210 new cases projected and 595,690 estimated deaths to occur due to cancer in 2016. Number of people surviving cancer (measured as 5-year survival rat...

Do nucleic acids moonlight as molecular chaperones?

Organisms use molecular chaperones to combat the unfolding and aggregation of proteins. While protein chaperones have been widely studied, here we demonstrate that DNA and RNA exhibit potent chaperone activity in vitro Nucleic acids suppress the aggregation of classic chaperone substrates up to 300-fold more effectively than the protein chaperone GroEL. Additionally, RNA cooperates with the Dna...

Molecular Chaperones as Prognostic Markers of Neuroblastoma

Molecular chaperones as HSF1-specific transcriptional repressors.

The rapid yet transient transcriptional activation of heat shock genes is mediated by the reversible conversion of HSF1 from an inert negatively regulated monomer to a transcriptionally active DNA-binding trimer. During attenuation of the heat shock response, transcription of heat shock genes returns to basal levels and HSF1 reverts to an inert monomer. These events coincide with elevated level...

Molecular Chaperones

In most cases proteins fold spontaneously under physiological conditions and do not require any external assistance. This has become evident since the experiments on ribonuclease A conducted by Anfinsen in ‘50s and ‘60s. The list of such “successful” folders has grown since and now includes many two-state proteins catalogued in Folding & Design 3, R81. These proteins fold rapidly and reliably t...