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Complementary role of two fragments of domain V of 23 S ribosomal RNA in protein folding
S PAL, S CHANDRA, S CHOWDHURY, D SARKAR, A N GHOSH, GUPTA C DAS
Published in AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
1999
Volume: 274
   
Issue: 46
Pages: 32771 - 32777
Abstract
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).
About the journal
JournalJournal of Biological Chemistry
PublisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN0021-9258
Open AccessYes