PMID:8104102: Difference between revisions
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!align=left |Citation | |||
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'''Horwich, AL, Low, KB, Fenton, WA, Hirshfield, IN and Furtak, K''' (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. ''Cell'' '''74''':909-17 | |||
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!align=left |Abstract | |||
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A general role for chaperonin ring structures in mediating folding of newly translated proteins has been suggested. Here we have directly examined the role of the E. coli chaperonin GroEL in the bacterial cytoplasm by production of temperature-sensitive lethal mutations in this essential gene. After shift to nonpermissive temperature, the rate of general translation in the mutant cells was reduced, but, more specifically, a defined group of cytoplasmic proteins--including citrate synthase, ketoglutarate dehydrogenase, and polynucleotide phosphorylase--were translated but failed to reach native form. Similarly, a monomeric test protein, maltose-binding protein, devoid of its signal domain, was translated but failed to fold to its native conformation. We conclude that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8104102 PubMed] | |||
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!align=left |Keywords | |||
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ATP-Binding Cassette Transporters; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/genetics; Bacteriophage lambda/metabolism; Carrier Proteins/biosynthesis; Carrier Proteins/genetics; Chaperonin 60; Citrate (si)-Synthase/biosynthesis; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Ketoglutarate Dehydrogenase Complex/biosynthesis; Maltose/metabolism; Maltose-Binding Proteins; Methionine; Monosaccharide Transport Proteins; Operon; Ornithine Carbamoyltransferase/biosynthesis; Ornithine Carbamoyltransferase/genetics; Plasmids; Polyribonucleotide Nucleotidyltransferase/biosynthesis; Promoter Regions, Genetic; Protein Biosynthesis; Protein Folding; Protein Sorting Signals/metabolism; Sequence Deletion; Temperature; Transduction, Genetic | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<annotationlinks/> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
{{LitLinks}} | |||
==See also== | |||
==References== | |||
{{RefHelp}} | |||
<references/> | |||
Latest revision as of 14:38, 5 July 2014
| Citation |
Horwich, AL, Low, KB, Fenton, WA, Hirshfield, IN and Furtak, K (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74:909-17 |
|---|---|
| Abstract |
A general role for chaperonin ring structures in mediating folding of newly translated proteins has been suggested. Here we have directly examined the role of the E. coli chaperonin GroEL in the bacterial cytoplasm by production of temperature-sensitive lethal mutations in this essential gene. After shift to nonpermissive temperature, the rate of general translation in the mutant cells was reduced, but, more specifically, a defined group of cytoplasmic proteins--including citrate synthase, ketoglutarate dehydrogenase, and polynucleotide phosphorylase--were translated but failed to reach native form. Similarly, a monomeric test protein, maltose-binding protein, devoid of its signal domain, was translated but failed to fold to its native conformation. We conclude that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures. |
| Links | |
| Keywords |
ATP-Binding Cassette Transporters; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/genetics; Bacteriophage lambda/metabolism; Carrier Proteins/biosynthesis; Carrier Proteins/genetics; Chaperonin 60; Citrate (si)-Synthase/biosynthesis; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Ketoglutarate Dehydrogenase Complex/biosynthesis; Maltose/metabolism; Maltose-Binding Proteins; Methionine; Monosaccharide Transport Proteins; Operon; Ornithine Carbamoyltransferase/biosynthesis; Ornithine Carbamoyltransferase/genetics; Plasmids; Polyribonucleotide Nucleotidyltransferase/biosynthesis; Promoter Regions, Genetic; Protein Biosynthesis; Protein Folding; Protein Sorting Signals/metabolism; Sequence Deletion; Temperature; Transduction, Genetic |
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