Who chaperones nascent chains in bacteria?
The physiological roles of the molecular chaperones trigger factor and DnaK in de novo protein folding have been unclear, but two new studies have shown that they perform essential, yet partially redundant, functions in chaperoning nascent protein chains in bacteria.
Pfanner
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Institut für Biochemie und Molekularbiologie Universität Freiburg Hermann-Herder-Strasse 7, D-79104, Freiburg, Germany. pfanner@uni-freiburg.de.
D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000502:physiology; D018834:Chaperonin 60 / Q000737:chemistry / Q000502:physiology; D003600:Cytosol / Q000737:chemistry; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology; D018832:Molecular Chaperones / Q000502:physiology*; D019696:Peptidylprolyl Isomerase / Q000502:physiology; D014176:Protein Biosynthesis / Q000502:physiology; D017510:Protein Folding
D001426:Bacterial Proteins; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; C063842:dnaK protein, E coli; D019696:Peptidylprolyl Isomerase