Abstract
Ribosome-inactivating proteins (RIPs) function to inhibit protein synthesis through the removal of specific adenine residues from eukaryotic ribosomal RNA and rending the 60S subunit unable to bind elongation factor 2. They have received much attention in biological and biomedical research due to their unique activities toward tumor cells, as well as the important roles in plant defense. Alpha-momorcharin (α-MC), a member of the type I family of RIPs, is rich in the seeds of Momordica charantia L. Previous studies demonstrated that α-MC is an effective antifungal and antibacterial protein. In this study, a detailed analysis of the DNase-like activity of α-MC was conducted. Results showed that the DNase-like activity toward plasmid DNA was time-dependent, temperature-related, and pH-stable. Moreover, a requirement for divalent metal ions in the catalytic domain of α-MC was confirmed. Additionally, Tyr93 was found to be a critical residue for the DNase-like activity, while Tyr134, Glu183, Arg186, and Trp215 were activity-related residues. This study on the chemico-physical properties and mechanism of action of α-MC will improve its utilization in scientific research, as well as its potential industrial uses. These results may also assist in the characterization and elucidation of the DNase-like enzymatic properties of other RIPs.
Keywords: Active residue, activity-related residues, alpha-momorcharin, DNase-like activity, polynucleotide: adenosine glycosidase activity, ribosome-inactivating proteins.
Protein & Peptide Letters
Title:Alpha-momorcharin: A Ribosome-Inactivating Protein from Momordica charantia, Possessing DNA Cleavage Properties
Volume: 20 Issue: 11
Author(s): Shuzhen Wang, Yinzhen Zheng, Junjie Yan, Zhixuan Zhu, Zhihua Wu and Yi Ding
Affiliation:
Keywords: Active residue, activity-related residues, alpha-momorcharin, DNase-like activity, polynucleotide: adenosine glycosidase activity, ribosome-inactivating proteins.
Abstract: Ribosome-inactivating proteins (RIPs) function to inhibit protein synthesis through the removal of specific adenine residues from eukaryotic ribosomal RNA and rending the 60S subunit unable to bind elongation factor 2. They have received much attention in biological and biomedical research due to their unique activities toward tumor cells, as well as the important roles in plant defense. Alpha-momorcharin (α-MC), a member of the type I family of RIPs, is rich in the seeds of Momordica charantia L. Previous studies demonstrated that α-MC is an effective antifungal and antibacterial protein. In this study, a detailed analysis of the DNase-like activity of α-MC was conducted. Results showed that the DNase-like activity toward plasmid DNA was time-dependent, temperature-related, and pH-stable. Moreover, a requirement for divalent metal ions in the catalytic domain of α-MC was confirmed. Additionally, Tyr93 was found to be a critical residue for the DNase-like activity, while Tyr134, Glu183, Arg186, and Trp215 were activity-related residues. This study on the chemico-physical properties and mechanism of action of α-MC will improve its utilization in scientific research, as well as its potential industrial uses. These results may also assist in the characterization and elucidation of the DNase-like enzymatic properties of other RIPs.
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Cite this article as:
Wang Shuzhen, Zheng Yinzhen, Yan Junjie, Zhu Zhixuan, Wu Zhihua and Ding Yi, Alpha-momorcharin: A Ribosome-Inactivating Protein from Momordica charantia, Possessing DNA Cleavage Properties, Protein & Peptide Letters 2013; 20 (11) . https://dx.doi.org/10.2174/09298665113209990048
DOI https://dx.doi.org/10.2174/09298665113209990048 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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