A Single-Ring Mitochondrial Chaperonin (Hsp60-Hsp10) Can Substitute for GroEL-GroES In Vivo
1999 ◽
Vol 181
(18)
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pp. 5871-5875
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Keyword(s):
ABSTRACT 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 colistrain 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.
1994 ◽
Vol 125
(5)
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pp. 989-996
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Keyword(s):
2007 ◽
Vol 39
(3)
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pp. 660
Keyword(s):
2006 ◽
Vol 38
(11)
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pp. 1975-1985
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1985 ◽
Vol 164
(2)
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pp. 665-673
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Keyword(s):
2020 ◽
Vol 83
(4)
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pp. 24-30
Keyword(s):
1976 ◽
Vol 17
(3)
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pp. 756-761
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