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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Philosophical transactions of the Royal Society of London. Series B, Biological sciences

Nascent chains: folding and chaperone interaction during elongation on ribosomes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Philosophical transactions of the Royal Society of London. Series B, Biological sciences - 29 Apr 1995

Tokatlidis K, Friguet B, Deville-Bonne D, Baleux F, Fedorov AN, Navon A, Djavadi-Ohaniance L, Goldberg ME

Link to Pubmed [PMID] – 7770491

Philos. Trans. R. Soc. Lond., B, Biol. Sci. 1995 Apr;348(1323):89-95

Monoclonal antibodies that detect folding intermediates in vitro were used to monitor the appearance of folded polypeptide chains during their synthesis on the ribosomes. Nascent immunoreactive chains of the bacteriophage P22 tail-spike protein and of the Escherichia coli beta 2 subunit of tryptophan-synthase were thus identified, suggesting that they can fold on the ribosomes. Moreover, the immunoreactivity of ribosome-bound tryptophan-synthase beta-chains of intermediate lengths was shown to appear with no detectable delay compared to their synthesis. This suggested that beta-chains start folding during their elongation on the ribosomes. However, newly synthesized incomplete beta-chains were shown to interact with chaperones while still bound to the ribosome. Because of the peculiar properties of the epitope recognized by the anti-tryptophan-synthase monoclonal antibody used, it could not be concluded whether the immunoreactivity of the nascent beta-chains resulted from their ability to fold cotranslationally or from their association with chaperones which might maintain them in an unfolded, immunoreactive state.

https://www.ncbi.nlm.nih.gov/pubmed/7770491