Molecular Mechanism of Hsp70 Chaperones: Interactions with Cochaperones and Substrates

Description

This lecture delves into the molecular mechanism of Hsp70 chaperones, focusing on their interactions with cochaperones and substrates. Topics covered include the structure and mode of action of Hsp70, allosteric regulation, probing the kinetics of ATP-induced conformational changes, and the influence of cochaperones like GrpE and DnaJ on the dynamics of DnaK. The lecture also explores the conformational equilibria in both nucleotide states, the impact of substrates on DnaK-ATP dynamics, and the unfolding of protein clients by Hsp70-Hdj1. Additionally, it discusses the regulation of the heat shock response by HSF1, including the chaperone titration model and the thermosensing properties of HSF1.

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Adenosine triphosphate

Adenosine triphosphate (ATP) is an organic compound that provides energy to drive and support many processes in living cells, such as muscle contraction, nerve impulse propagation, condensate dissolution, and chemical synthesis. Found in all known forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP.

ATP synthase

ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (Pi). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is: ADP + Pi + 2H+out ATP + H2O + 2H+in ATP synthase lies across a cellular membrane and forms an aperture that protons can cross from areas of high concentration to areas of low concentration, imparting energy for the synthesis of ATP.

Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.

Heat shock response

The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. In a normal cell, proteostasis (protein homeostasis) must be maintained because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order to perform their biological functions.

Heat shock protein

Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.