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 chaperonins, in the assembly of phage and multisubunit proteins. 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 product. Over-expression of the groE operon in E. coli causes enhanced assembly of heterologously expressed ribulose bisphosphate carboxylase subunits and suppresses the heat-sensitive mutant phenotype of several dnaA alleles. 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 origin. 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 proteins, in the folding-assembly pathways of many proteins.
|
Authors | T K Van Dyk, A A Gatenby, R A LaRossa |
Journal | Nature
(Nature)
Vol. 342
Issue 6248
Pg. 451-3
(Nov 23 1989)
ISSN: 0028-0836 [Print] England |
PMID | 2573840
(Publication Type: Journal Article)
|
Chemical References |
- Bacterial Proteins
- Codon
- Proteins
- Chaperonins
|
Topics |
- Alleles
- Bacterial Proteins
(genetics, metabolism)
- Chaperonins
- Codon
(genetics)
- Escherichia coli
(genetics)
- Genes, Bacterial
- Mutation
- Operon
- Phenotype
- Plasmids
- Proteins
(genetics, metabolism)
- Salmonella Phages
(genetics)
- Salmonella typhimurium
(genetics)
- Suppression, Genetic
|