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Demonstration by genetic suppression of interaction of GroE products with many proteins

Nature volume 342, pages 451–453 (1989)Cite this article

Abstract

THE way in which proteins attain and maintain their final form is of fundamental importance. Recent work has focused on the role of a set of ubiquitous proteins, termed chaperonins1, in the assembly of phage2 and multisubunit proteins3,4. The range of chaperonin action is unknown; they could interact with most cellular polypeptides or have a limited subset of protein partners. Included in the chaperonin family is the essential heat-shock regulated Escherichia coli groEL gene product1, 5 ,6. Over-expression of the groE operon in E. coli causes enhanced assembly of heterologously expressed ribulose bisphosphate carboxylase subunits3 and suppresses the heat-sensitive mutant phenotype of several dnaA alleles7, 8. It has been inferred that suppression of heat-sensitive mutations is confined to dnaA alleles and that this confinement could reflect an interaction between the groE operon products and a dnaA protein aggregate at the replication origin7, 9. We now report that multiple copies of the groE operon suppress mutations in genes encoding several diverse proteins. Our data indicate a general role for the groE operon products, the GroEL and GroES proteins10, in the folding–assembly pathways of many proteins.

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Author notes

  1. Robert A. LaRossa: To whom correspondence should be addressed.

Authors and Affiliations

  1. Central Research and Development Department, E. I. du Pont de Nemours and Company, Experimental Station, PO Box 80328, Wilmington, Delaware, 19880-0328, USA

    Tina K. Van Dyk, Anthony A. Gatenby & Robert A. LaRossa

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  1. Tina K. Van Dyk
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  2. Anthony A. Gatenby
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  3. Robert A. LaRossa
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Van Dyk, T., Gatenby, A. & LaRossa, R. Demonstration by genetic suppression of interaction of GroE products with many proteins. Nature 342, 451–453 (1989). https://doi.org/10.1038/342451a0

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