The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.
ClpB and Hsp104 (ClpB/Hsp104) are essential proteins of the heat-shock response and belong to the class 1 family of Clp/Hsp100 AAA+ ATPases. Members of this family form large ring structures and contain two AAA+ modules, which consist of a RecA-like nucleotide-binding domain (NBD) and an alpha-helical domain. Furthermore, ClpB/Hsp104 has a longer middle region, the ClpB/Hsp104-linker, which is essential for chaperone activity. Unlike other Clp/Hsp100 proteins, however, ClpB/Hsp104 neither associates with a cellular protease nor directs the degradation of its substrate proteins. Rather, ClpB/Hsp104 is a bona fide molecular chaperone, which has the remarkable ability to rescue proteins from an aggregated state. The full recovery of these proteins requires the assistance of the cognate DnaK/Hsp70 chaperone system. The mechanism of this "bi-chaperone" network, however, remains elusive. Here we review the current understanding of the structure-function relationship of the ClpB/Hsp104 molecular chaperone and its role in protein disaggregation.
Lee
Sukyeong
S
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston TX, 77030, USA.
Sowa
Mathew E
ME
Choi
Jae-Mun
JM
Tsai
Francis T F
FT
D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000502:physiology*; D018832:Molecular Chaperones / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D020673:Protein Renaturation
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones