A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.
Chaperonins participate in the facilitated folding of a variety of proteins in vivo. To see whether the same spectrum of target proteins can be productively folded by the double-ring prokaryotic chaperonin GroEL-GroES and its single-ring human mitochondrial homolog, Hsp60-Hsp10, we expressed the latter in an Escherichia coli strain engineered so that the groE operon is under strict regulatory control. We found that expression of Hsp60-Hsp10 restores viability to cells that no longer express GroEL-GroES, formally demonstrating that Hsp60-Hsp10 can carry out all essential in vivo functions of GroEL-GroES.
Nielsen
K L
KL
Department of Biochemistry, New York University Medical Center, New York, New York 10016, USA.
McLennan
N
N
Masters
M
M
Cowan
N J
NJ
D018835:Chaperonin 10 / Q000235:genetics / Q000378:metabolism*; D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development; D005818:Genetic Engineering; D006801:Humans; D008928:Mitochondria / Q000235:genetics; D009876:Operon; D011994:Recombinant Proteins / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D011994:Recombinant Proteins