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 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).
Pal
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S
Department of Biophysics, University College of Science and Technology, University of Calcutta, 92 Acharya Prafulla Chandra Road, Calcutta 700009, India.
Chandra
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Chowdhury
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Sarkar
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D
Ghosh
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AN
Gupta
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CD
D000818:Animals; D001412:Bacillus subtilis / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000378:metabolism; D002850:Chromatography, Gel; D004789:Enzyme Activation; D005453:Fluorescence; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D009690:Nucleic Acid Conformation; D009843:Oligoribonucleotides / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D012329:RNA, Bacterial / Q000378:metabolism; D012338:RNA, Ribosomal, 23S / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013552:Swine; D014364:Tryptophan / Q000737:chemistry
D009843:Oligoribonucleotides; D012329:RNA, Bacterial; D012338:RNA, Ribosomal, 23S; D014364:Tryptophan; D007770:L-Lactate Dehydrogenase; D002256:Carbonic Anhydrases