Abstract
Although accumulating evidence has revealed that most proteins can fold without the assistance of molecular chaperones, little attention has been paid to other types of chaperoning macromolecules. A variety of proteins interact with diverse RNA molecules in vivo, suggesting a potential role of RNAs for folding of their interacting proteins. Here we show that the in vitro refolding of a representative molecular chaperone, DnaK, an Escherichia coli homolog of Hsp70, could be assisted by its interacting 5S rRNA. The folding enhancement occurred in RNA concentration and its size dependent manner whereas neither the RNA with the reverse sequence of 5S rRNA nor the RNase pretreated 5S rRNA stimulated the folding in vitro. Based on our results, we propose that 5S rRNA could exert the chaperoning activity on DnaK during the folding process. The results suggest an interesting possibility that the folding of RNA-interacting proteins could be assisted by their cognate RNA ligands.
| Original language | English |
|---|---|
| Pages (from-to) | 1177-1181 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 391 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2010 Jan 8 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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5S rRNA-assisted DnaK refolding. / Kim, Hyo Kyung; Choi, Seong Il; Seong, Baik L.
In: Biochemical and Biophysical Research Communications, Vol. 391, No. 2, 08.01.2010, p. 1177-1181.Research output: Contribution to journal › Article
TY - JOUR
T1 - 5S rRNA-assisted DnaK refolding
AU - Kim, Hyo Kyung
AU - Choi, Seong Il
AU - Seong, Baik L.
PY - 2010/1/8
Y1 - 2010/1/8
N2 - Although accumulating evidence has revealed that most proteins can fold without the assistance of molecular chaperones, little attention has been paid to other types of chaperoning macromolecules. A variety of proteins interact with diverse RNA molecules in vivo, suggesting a potential role of RNAs for folding of their interacting proteins. Here we show that the in vitro refolding of a representative molecular chaperone, DnaK, an Escherichia coli homolog of Hsp70, could be assisted by its interacting 5S rRNA. The folding enhancement occurred in RNA concentration and its size dependent manner whereas neither the RNA with the reverse sequence of 5S rRNA nor the RNase pretreated 5S rRNA stimulated the folding in vitro. Based on our results, we propose that 5S rRNA could exert the chaperoning activity on DnaK during the folding process. The results suggest an interesting possibility that the folding of RNA-interacting proteins could be assisted by their cognate RNA ligands.
AB - Although accumulating evidence has revealed that most proteins can fold without the assistance of molecular chaperones, little attention has been paid to other types of chaperoning macromolecules. A variety of proteins interact with diverse RNA molecules in vivo, suggesting a potential role of RNAs for folding of their interacting proteins. Here we show that the in vitro refolding of a representative molecular chaperone, DnaK, an Escherichia coli homolog of Hsp70, could be assisted by its interacting 5S rRNA. The folding enhancement occurred in RNA concentration and its size dependent manner whereas neither the RNA with the reverse sequence of 5S rRNA nor the RNase pretreated 5S rRNA stimulated the folding in vitro. Based on our results, we propose that 5S rRNA could exert the chaperoning activity on DnaK during the folding process. The results suggest an interesting possibility that the folding of RNA-interacting proteins could be assisted by their cognate RNA ligands.
UR - http://www.scopus.com/inward/record.url?scp=73449133327&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=73449133327&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2009.11.176
DO - 10.1016/j.bbrc.2009.11.176
M3 - Article
C2 - 19962961
AN - SCOPUS:73449133327
VL - 391
SP - 1177
EP - 1181
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -