Abstract：
:Rhodanese bound to bacterial ribosomes as peptidyl-tRNA can be folded into an enzymatically active conformation by generating C-terminal extensions of the wild-type enzyme. Rhodanese was synthesized by coupled transcription/translation in a cell-free Escherichia coli system from plasmids containing the coding sequences for the wild-type enzyme or its C-terminally extended mutants. Two proteins with extensions of 23 amino acids or longer were enzymatically active while bound to the ribosomes whereas wild-type protein and a 13-amino acid extension were not. All forms of the enzyme were active after termination and release of the full-length protein from the ribosomes. All five of the bacterial chaperones were required to substantially increase the specific enzymatic activity of the extended rhodanese while the nascent protein was bound to ribosomes. The results provide direct support for the hypothesis that proteins acquire tertiary structure as they are formed in ribosomes.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kudlicki W,Chirgwin J,Kramer G,Hardesty Bdoi
10.1021/bi00044a003subject
Has Abstractpub_date
1995-11-07 00:00:00pages
14284-7issue
44eissn
0006-2960issn
1520-4995journal_volume
34pub_type
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