Document Detail

Circular dichroism and the secondary structure of the ROF2 protein from Arabidopsis thaliana.
MedLine Citation:
PMID:  23996408     Owner:  NLM     Status:  MEDLINE    
The protein ROF2 from the plant Arabidopsis thaliana acts as a heat stress modulator, being involved in the long-term acquired thermotolerance of the plant. Here we investigate the relationship between the biological function and the structure of ROF2, inferred by circular dichroism (CD) spectroscopy. The far-UV CD spectra, analyzed with the CDPro and DICHROWEB program packages, yield the percentages of α-helices, β-sheets, unordered regions, turns and poly(Pro)II-helices in the secondary structure of ROF2. According to the analysis, the percentages of the structural elements of ROF2 are about 40% for β-sheets, 30% for unordered regions, 17% for turns, 10% for poly(Pro)II-helices and 3% for α-helices. The near-UV CD spectra suggest that ROF2 proteins can associate, forming super-secondary structures. Our CD experiments performed at temperatures between 5 °C and 97 °C indicate that the thermal denaturation of ROF2 caused by a raise in temperature up to 55 °C is followed by a thermal refolding of the protein as the temperature is raised further. The new secondary structure, acquired around 65 °C, remains stable up to 97 °C. The structural stability of ROF2 at high temperatures might play an important role in the experimentally observed thermotolerance of Arabidopsis thaliana.
Liliana Lighezan; David Meiri; Adina Breiman; Adrian Neagu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-06-19
Journal Detail:
Title:  Journal of biological physics     Volume:  39     ISSN:  1573-0689     ISO Abbreviation:  J Biol Phys     Publication Date:  2013 Sep 
Date Detail:
Created Date:  2013-09-02     Completed Date:  2014-07-03     Revised Date:  2014-09-02    
Medline Journal Info:
Nlm Unique ID:  0417731     Medline TA:  J Biol Phys     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  635-48     Citation Subset:  IM    
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MeSH Terms
Arabidopsis Proteins / chemistry*
Circular Dichroism
Peptidylprolyl Isomerase / chemistry*
Protein Stability
Protein Structure, Secondary
Reg. No./Substance:
0/Arabidopsis Proteins; EC Isomerase; EC protein, Arabidopsis

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