Abstract
Artemin is an abundant thermostable protein in Artemia encysted embryos under stress. It is considered as a stress protein, as its highly regulated expression is associated with stress resistance in this crustacea. In the present study, artemin has been shown to be a potent molecular chaperone with high efficacy. Artemin is capable of inhibiting the chemical aggregation of proteins such as carbonic anhydrase (CA) and horseradish peroxidase (HRP) at unique molar ratios of chaperone to substrates (1:40 and 1:26 for CA and HRP, respectively). Furthermore, it can also enhance refolding yield of these substrates by nearly 50%. The refolding promotion of CA is checked and verified through a sensitive fluorimetric technique. Based on these experiments, artemin showed higher chaperone activity than other chaperones. The evaluation of artemin surface using ANS showed it to be highly hydrophobic, probably resulting in its high efficacy. These results suggest that artemin can be considered a novel low molecular weight chaperone.
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Abbreviations
- ADH:
-
Alcohol dehydrogenase
- ANS:
-
1-aniline-8-naphthalene-sulfonate
- ASA:
-
Accessible surface area
- CA:
-
Carbonic anhydrase
- CS:
-
Citrate synthase
- DNSA:
-
5-dimethylaminonaphtalene-1-sulfonamide
- FRET:
-
Fluorescence resonance energy transfer
- GdmCl:
-
Guanidinium chloride
- HRP:
-
Horseradish peroxidase
- HuTCTP:
-
Human translationally controlled tumor protein
- IPTG:
-
Isopropyl β-D-thiogalactopyranoside
- LB:
-
Luria-Bertani
- LEA:
-
Late embryogenesis abundant
- MDH:
-
Malate dehydrogenase
- Mj:
-
Methanococcus jannaschii
- Ni-NTA:
-
Nickel-nitrilotriacetic acid
- pNPAc:
-
p-nitrophenyl acetate
- PSH:
-
Protein surface hydrophobicity
- SCM:
-
Single-chain monellin
- sHSP:
-
Small heat shock protein
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Acknowledgments
We thank Professor James S. Clegg, Mr. Mehdi Rassa and Dr. Shahram Shahangian for their help. The authors express their gratitude to the Research Council of the University of Guilan and the Ministry of Science, Research and Technology for financial support during the course of this project.
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S. Shirin Shahangian and B. Rasti have contributed equally to this work.
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Shahangian, S.S., Rasti, B., Sajedi, R.H. et al. Artemin as an Efficient Molecular Chaperone. Protein J 30, 549–557 (2011). https://doi.org/10.1007/s10930-011-9359-4
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DOI: https://doi.org/10.1007/s10930-011-9359-4