Importance of Glu53 in the C-terminal region of brazzein, a sweet-tasting protein
BACKGROUND The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C‐terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires furt...
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| Published in | Journal of the science of food and agriculture Vol. 96; no. 9; pp. 3202 - 3206 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.07.2016
John Wiley and Sons, Limited |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-5142 1097-0010 |
| DOI | 10.1002/jsfa.7501 |
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| Abstract | BACKGROUND
The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C‐terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study.
RESULTS
To identify important residues responsible for the sweetness of the protein brazzein, four mutants of the Glu53 residue in the C‐terminal region of des‐pE1M‐brazzein, which lacks the N‐terminal pyroglutamate, were constructed using site‐directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des‐pE1M‐brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des‐pE1M‐brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein.
CONCLUSION
Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet‐taste receptor. © 2015 Society of Chemical Industry |
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| AbstractList | BACKGROUND The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C-terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study. RESULTS To identify important residues responsible for the sweetness of the protein brazzein, four mutants of the Glu53 residue in the C-terminal region of des-pE1M-brazzein, which lacks the N-terminal pyroglutamate, were constructed using site-directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des-pE1M-brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des-pE1M-brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein. CONCLUSION Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet-taste receptor. BACKGROUND The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C‐terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study. RESULTS To identify important residues responsible for the sweetness of the protein brazzein, four mutants of the Glu53 residue in the C‐terminal region of des‐pE1M‐brazzein, which lacks the N‐terminal pyroglutamate, were constructed using site‐directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des‐pE1M‐brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des‐pE1M‐brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein. CONCLUSION Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet‐taste receptor. © 2015 Society of Chemical Industry The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C-terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study. To identify important residues responsible for the sweetness of the protein brazzein, four mutants of the Glu53 residue in the C-terminal region of des-pE1M-brazzein, which lacks the N-terminal pyroglutamate, were constructed using site-directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des-pE1M-brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des-pE1M-brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein. Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet-taste receptor. © 2015 Society of Chemical Industry. BACKGROUND The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues in the C-terminus of brazzein are known to play a critical role in sweetness, the currently unknown function of Glu53 requires further study. RESULTS To identify important residues responsible for the sweetness of the protein brazzein, four mutants of the Glu53 residue in the C-terminal region of des-pE1M-brazzein, which lacks the N-terminal pyroglutamate, were constructed using site-directed mutagenesis. Mutations of Glu53 substitution to Ala or Asp significantly decreased the sweetness. On the other hand, a Lys mutation resulted in a molecule with sweetness similar to that of des-pE1M-brazzein. Mutation of Glu53 to Arg resulted in a molecule significantly sweeter than des-pE1M-brazzein, which agrees with previous findings showing that mutation with positively charged residues results in a sweeter protein. CONCLUSION Our results suggest that the residue at position 53 is crucial for the sweetness of brazzein, which may be interacting with the sweet-taste receptor. © 2015 Society of Chemical Industry |
| Author | Kong, Ji-Na Jang, Jin-Chul Kong, Kwang-Hoon Lim, Jin-Kyung Kim, Myung-Chul |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26478244$$D View this record in MEDLINE/PubMed |
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| References_xml | – reference: Nagata K, Hongo N, Kameda Y, Yamamura A, Sasaki H, Lee WC et al., The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana. Acta Cryst D69:642-647 (2013). – reference: Yoon SY, Kong JN, Jo DH and Kong KH, Residue mutations in the sweetness loops for the sweet-tasting protein brazzein. Food Chem 129:1327-1330 (2011). – reference: Lee JW, Cha JE, Jo HJ and Kong KH, Multiple mutations of the critical amino acid residues for the sweetness of the sweet-tasting protein, brazzein. Food Chem 138:1370-1373 (2013). – reference: Ming D, Hellekant G and Zhong H, Characterization and chemical modification of brazzein, a high potency thermostable sweet protein from Pentadiplandra brazzeana. Acta Bot Yunnancia 18:123-133 (1996). – reference: Assadi-Porter FM, Tonelli M, Maillet EL, Markely JL and Max M, Interactions between the human sweet-sensing T1R2-T1R3 receptor and sweeteners detected by saturation transfer difference NMR spectroscopy. Biochim Biophys Acta 1798:82-86 (2010). – reference: Lee JJ, Kong JN, Do HD, Jo DH and Kong KH, Design and efficient soluble expression of a sweet protein, brazzein and minor-form mutant. Bull Korean Chem Soc 31:3830-3833 (2010). – reference: Temussi PA, Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor. FEBS Lett 526:1-4 (2002). – reference: Assadi-Porter FM, Abildgaard F, Blad H, Cornilescu CC and Markely JL, Brazzein, a small, sweet protein: effect of mutation on its structure, dynamics and functional properties. Chem Senses 30(Suppl 1):i90-i91 (2005). – reference: Wintjens R, Viet TMVN, Mbosso E and Huet J, Hypothesis/review: the structural basis of sweetness perception of sweet-tasting plant proteins can be deduced from sequence analysis. Plant Sci 181:347-354 (2011). – reference: Assadi-Porter FM, Abildgaard F, Blad H and Markley JL, Correlation of the sweetness of variants of the protein brazzein with patterns of hydrogen bonds detected by NMR spectroscopy. J Biol Chem 278:31331-31339 (2003). – reference: Walters DE and Hellekant G, Interactions of the sweet protein brazzein with the sweet taste receptor. J Agric Food Chem 54:10129-10133 (2006). – reference: Temussi PA, Natural sweet macromolecules: how sweet proteins work. Cell Mol Life Sci 63:1876-1888 (2006). – reference: Esposito V, Gallucci R, Picone D, Saviano G, Tancredi T and Temussi PA, The importance of electrostatic potential in the interaction of sweet proteins with the sweet taste receptor. J Mol Biol 360:448-456 (2006). – reference: Kaneko R and Kitabatake N, Sweetness of sweet protein thaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions. Biosci Biotechnol Biochem 65:409-413 (2001). – reference: Ohta K, Masuda T, Ide N and Kitabatake N, Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I. FEBS J 275:3644-3652 (2008). – reference: Assadi-Porter FM, Aceti DJ and Markley JL, Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. Arch Biochem Biophys 376:259-265 (2000). – reference: Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC et al., UCSF Chimera: a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612 (2004). – reference: Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G and Markley JL, Solution structure of the thermostable sweet-tasting protein brazzein. 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The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the... The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the residues... BACKGROUND The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As the... BACKGROUND: The sweetness of brazzein, one of the known sweet proteins, is dependent on charges and/or structures of its specific amino acid side chains. As... |
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| SubjectTerms | Amino Acid Motifs Amino Acid Substitution - genetics Amino acids Arginine - chemistry brazzein Construction Escherichia coli - genetics Food science Foods Gene Expression Regulation Glu53 Glutamine - chemistry Models, Molecular mutagenesis Mutagenesis, Site-Directed mutants Mutations Plant Proteins - chemistry Plant Proteins - genetics Protein Conformation protein sweeteners Proteins Receptors Residues Sensory perception Sequence Analysis, Protein site-directed mutagenesis Structure-Activity Relationship Sweetening Agents - chemistry sweetness sweetness determinant Sweets Taste |
| Title | Importance of Glu53 in the C-terminal region of brazzein, a sweet-tasting protein |
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