Cooperation between heat shock proteins in organizing of proteins spatial structure
Journal Title: Advances in Hygiene and Experimental Medicine - Year 2014, Vol 68, Issue
Abstract
Heat shock proteins (Hsps) are a class of proteins with highly conserved amino acid sequences. They are widespread in nature; they are found in archeons, true bacteria and eukaryotic organisms. Hsps from various families, commonly interact to execute essential cellular tasks, such as molecular regulation of newly synthesized protein-folding or restoration of the appropriate conformation of denatured and aggregated proteins. In this review we discuss mechanisms of spatial organization of protein structure mediated by Hsp10, Hsp40, Hsp60, Hsp70, Hsp104 (Hsp100) and Hsp110. Interactions between Hsps of different molecular weights are described.
Authors and Affiliations
Zbigniew Wyżewski, Karolina P. Gregorczyk, Lidia Szulc-Dąbrowska, Justyna Struzik, Joanna Szczepanowska, Marek Niemiałtowski
Keywords
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