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Protein Solubility and Folding Enhancement by Interaction with RNA

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Authors
Choi, Seong Il; Han, Kyoung Sim; Kim, Chul Woo; Ryu, Ki-Sun; Kim, Byung Hee; Kim, Kyun-Hwan; Kim, Seo-Il; Kang, Tae Hyun; Shin, Hang-Cheol; Lim, Keo-Heun; Kim, Hyo Kyung; Hyun, Jeong-Min; Seong, Baik L.
Issue Date
2008-07-16
Publisher
Public Library of Science
Citation
PLoS ONE 3(7): e2677
Abstract
While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated by interaction with RNA. When an RNA-binding module is placed at the N-terminus of aggregation-prone target proteins, this module, upon binding with RNA, further promotes the solubility of passenger proteins, potentially leading to enhancement of proper protein folding. Studies on in vitro refolding in the presence of RNA, coexpression of RNA molecules in vivo and the mutants with impaired RNA binding ability suggests that RNA can exert chaperoning effect on their bound proteins. The results suggest that RNA binding could affect the overall kinetic network of protein folding pathway in favor of productive folding over off-pathway aggregation. In addition, the RNA binding-mediated solubility enhancement is extremely robust for increasing soluble yield of passenger proteins and could be usefully implemented for high-throughput protein expression for functional and structural genomic research initiatives. The RNA-mediated chaperone type presented here would give new insights into de novo folding in vivo.
ISSN
1932-6203
Language
English
URI
http://www.plosone.org
http://hdl.handle.net/10371/3851
DOI
https://doi.org/10.1371/journal.pone.0002677.g001
https://doi.org/10.1371/journal.pone.0002677.g001
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College of Medicine/School of Medicine (의과대학/대학원)Pathology (병리학전공)Journal Papers (저널논문_병리학전공)
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