Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria

• Published in: Acta biochimica polonica Vol. 54; no. 2; pp. 245 - 252
• Main Authors: Zmijewski, Michał A, Skórko-Glonek, Joanna, Tanfani, Fabio, Banecki, Bogdan, Kotlarz, Agnieszka, Macario, Alberto J L, Lipińska, Barbara
• Format: Journal Article
• Language: English
• Published: Poland 01.01.2007
• Subjects: Archaea; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - metabolism; HSP70 Heat-Shock Proteins - chemistry; HSP70 Heat-Shock Proteins - metabolism; Methanosarcina - chemistry; Methanosarcina - metabolism; Methanosarcina mazei; Models, Molecular; Multiprotein Complexes; Protein Binding; Protein Structure, Secondary; Species Specificity; Spectroscopy, Fourier Transform Infrared

Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK)...