Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding Journal Article
| Authors: | Hayer-Hartl, M. K.; Martin, J.; Hartl, F. U. |
| Article Title: | Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding |
| Abstract: | The chaperonins GroEL and GroES of Escherichia coli facilitate protein folding in an adenosine triphosphate (ATP)-dependent reaction cycle. The kinetic parameters for the formation and dissociation of GroEL-GroES complexes were analyzed by surface plasmon resonance. Association of GroES and subsequent ATP hydrolysis in the interacting GroEL toroid resulted in the formation of a stable GroEL:ADP:GroES complex. The complex dissociated as a result of ATP hydrolysis in the opposite GroEL toroid, without formation of a symmetrical GroEL:(GroES)2 intermediate. Dissociation was accelerated by the addition of unfolded polypeptide. Thus, the functional chaperonin unit is an asymmetrical GroEL:GroES complex, and substrate protein plays an active role in modulating the chaperonin reaction cycle. |
| Keywords: | controlled study; nonhuman; protein protein interaction; protein stability; adenosine diphosphate; bacterial protein; kinetics; serine endopeptidases; escherichia coli; adenosine triphosphate; protein folding; adenosine triphosphatase; hydrolysis; dissociation; hydrogen-ion concentration; magnesium; polypeptide; priority journal; article; support, u.s. gov't, p.h.s.; adenosinetriphosphatase; endopeptidase k; chaperonin; groel protein; groes protein |
| Journal Title: | Science |
| Volume: | 269 |
| Issue: | 5225 |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Date Published: | 1995-08-11 |
| Start Page: | 836 |
| End Page: | 841 |
| Language: | English |
| DOI: | 10.1126/science.7638601 |
| PUBMED: | 7638601 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 28 August 2018 -- Source: Scopus |
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