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Arginine, a Key Residue for the Enhancing Ability of an Antifreeze Protein of the Beetle Dendroides canadensis

Wang, Sen and Amornwittawat, Natapol and Juwita, Vonny and Kao, Yu and Duman, John G. and Pascal, Tod A. and Goddard, William A., III and Wen, Xin (2009) Arginine, a Key Residue for the Enhancing Ability of an Antifreeze Protein of the Beetle Dendroides canadensis. Biochemistry, 48 (40). pp. 9696-9703. ISSN 0006-2960. PMCID PMC2760095. https://resolver.caltech.edu/CaltechAUTHORS:20091022-130051821

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Abstract

Antifreeze proteins (AFPs) can produce a difference between the nonequilibrium freezing point and the melting point, termed thermal hysteresis (TH). The TH activity of an antifreeze protein (AFP) depends on the specific AFP and its concentration as well as the presence of cosolutes including low molecular mass solutes and/or proteins. We recently identified series of carboxylates and polyols as efficient enhancers for an AFP from the beetle Dendroides canadensis. In this study, we chemically modified DAFP-1 using the arginine-specific reagent 1,2-cyclohexanedione. We demonstrated that 1,2-cyclohexanedione specifically modifies one arginine residue and the modified DAFP-1 loses its enhancing ability completely or partially in the presence of previously identified enhancers. The stronger the enhancement ability of the enhancer on the native DAFP-1, the stronger the enhancement effect of the enhancer on the modified DAFP-1. The weaker enhancers (e.g., glycerol) completely lose their enhancement effect on the modified DAFP-1 due to their inability to compete with 1,2-cyclohexanedione for the arginine residue. Regeneration of the arginine residue using hydroxylamine fully restored the enhancing ability of DAFP-1. These studies indicated that an arginine residue is critical for the enhancing ability of DAFP-1 and the guanidinium group of the arginine residue is important for its interaction with the enhancers, where the general mechanism of arginine−ligand interaction is borne. This work may initiate a complete mechanistic study of the enhancement effect in AFPs.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bi901283pDOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi901283pPublisherArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760095/PubMed CentralArticle
ORCID:
AuthorORCID
Pascal, Tod A.0000-0003-2096-1143
Goddard, William A., III0000-0003-0097-5716
Additional Information:© 2009 American Chemical Society. Received July 26, 2009; Revised Manuscript Received September 6, 2009. Publication Date (Web): September 11, 2009. This study was supported by National Institutes of Health Grant 1SC3GM086249-01 and the NIH-RIMI program at California State University, Los Angeles (P20 MD001824-01). We thank the Protein and Nucleic Acid Facility at Stanford University, Stanford, CA, for MALDI-TOF mass spectrometry. VMD was developed by the Theoretical and Computational Biophysics Group in the Beckman Institute for Advanced Science and Technology at the University of Illinois at Urbana−Champaign. Supporting Information: HPLC profiles of the modification reaction of DAFP-1, the antifreeze activities of DAFP-1and the Arg-modified DAFP-1 in the presence of various enhancers, and MALDI-TOF mass spectrum of DAFP-1 incubated with citrate. This material is available free of charge via the Internet at http://pubs.acs.org.
Funders:
Funding AgencyGrant Number
NIH1SC3GM086249-01
NIHP20 MD001824-01
Issue or Number:40
PubMed Central ID:PMC2760095
Record Number:CaltechAUTHORS:20091022-130051821
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20091022-130051821
Official Citation:Arginine, a Key Residue for the Enhancing Ability of an Antifreeze Protein of the Beetle Dendroides canadensis Sen Wang, Natapol Amornwittawat, Vonny Juwita, Yu Kao, John G. Duman, Tod A. Pascal, William A. Goddard III, Xin Wen Biochemistry 2009 48 (40), 9696-9703
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:16456
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:22 Oct 2009 21:45
Last Modified:03 Oct 2019 01:12

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