GroEL and GroES Increase the Specific Enzymatic Activity of Newly-Synthesized Rhodanese If Present during in Vitro Transcription/Translation

Tamara Tsalkova, Gustavo Zardeneta, Wieslaw Kudlicki, Gisela Kramer, Paul M. Horowitz, Boyd Hardesty

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Enzymatically active mammalian rhodanese, a mitochondrial matrix enzyme, which has been found to require assistants for efficient refolding in vitro, has been synthesized from a plasmid in a cell-free, fractionated, coupled transcription/translation system derived from Escherichia coli. The bacterial chaperonins, GroEL and GroES, along with the rhodanese substrate thiosulfate greatly enhance the specific enzymatic activity of the rhodanese polypeptide that is formed. Indirect evidence suggests that the effect of the GroEL/ES chaperonins is on ribosome-bound nascent peptides. The in vitro transcription/translation system produces sufficient amounts of rhodanese to provide a system for studying factors that control the initial steps in folding of nascent proteins.

Original languageEnglish (US)
Pages (from-to)3377-3380
Number of pages4
JournalBiochemistry
Volume32
Issue number13
DOIs
StatePublished - Apr 1 1993
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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