Complementary Role of Two Fragments of Domain V of 23 S Ribosomal RNA in Protein Folding

We have shown that the domain V of bacterial 23 S rRNA could fold denatured proteins to their active state. This segment of 23 S rRNA could further be split into two parts. One part containing mainly the central loop of domain V could bind denatured human carbonic anhydrase I stably. This associatio...

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Bibliographic Details
Published in:The Journal of biological chemistry 1999-11, Vol.274 (46), p.32771-32777
Main Authors: Pal, Saumen, Chandra, Suparna, Chowdhury, Saheli, Sarkar, Dibyendu, Ghosh, A.N., Gupta, Chanchal Das
Format: Article
Language:English
Subjects:
Animals
Bacillus subtilis - metabolism
Carbonic Anhydrases - metabolism
Chromatography, Gel
Enzyme Activation
Fluorescence
Humans
L-Lactate Dehydrogenase - metabolism
Nucleic Acid Conformation
Oligoribonucleotides - metabolism
Protein Denaturation
Protein Folding
Ribosomes - metabolism
RNA, Bacterial - metabolism
RNA, Ribosomal, 23S - metabolism
rRNA 23S
Swine
Tryptophan - chemistry
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Summary:We have shown that the domain V of bacterial 23 S rRNA could fold denatured proteins to their active state. This segment of 23 S rRNA could further be split into two parts. One part containing mainly the central loop of domain V could bind denatured human carbonic anhydrase I stably. This association could be reversed by adding the other part of domain V. The released enzyme was directed in such a way by the central loop of domain V that it could now fold by itself to active form. This agrees with our earlier observation that proteins fold within the cell posttranslationally, a process that is completed after release of the newly synthesized polypeptide from the ribosome (Chattopadhyay, S., Pal, S., Chandra, S., Sarkar, D., and DasGupta, C. (1999) Biochim. Biophys. Acta 1429, 293–298).
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.274.46.32771