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Ribosome inactivating proteins from Rosaceae

(2016) MOLECULES. 21(8).
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Abstract
Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry. All RIP domains from Rosaceae share high sequence similarity with conserved residues in the catalytic site and the carbohydrate binding sites. The genomes of Malus domestica and Pyrus communis contain both type 1 and type 2 RIP sequences, whereas for Prunus mume, Prunus persica, Pyrus bretschneideri, and Pyrus communis a complex set of type 1 RIP sequences was retrieved. Heterologous expression and purification of the type 1 as well as the type 2 RIP from apple allowed to characterize the biological activity of the proteins. Both RIPs from Malus domestica can inhibit protein synthesis. Furthermore, molecular modelling suggests that RIPs from Rosaceae possess three-dimensional structures that are highly similar to the model proteins and can bind to RIP substrates. Screening of the recombinant type 2 RIP from apple on a glycan array revealed that this type 2 RIP interacts with terminal sialic acid residues. Our data suggest that the RIPs from Rosaceae are biologically active proteins.
Keywords
carbohydrate binding activity, molecular modeling, protein synthesis inhibition, ribosome-inactivating proteins, RICIN-A-CHAIN, ELDERBERRY SAMBUCUS-NIGRA, PLANTA ANTIVIRAL ACTIVITY, ACTIVE-SITE, MOMORDICA-CHARANTIA, TRANSGENIC TOBACCO, CRYSTAL-STRUCTURE, SIALIC-ACID, IRIS BULBS, IN-VIVO

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Citation

Please use this url to cite or link to this publication:

MLA
Shang, Chenjing, et al. “Ribosome Inactivating Proteins from Rosaceae.” MOLECULES, vol. 21, no. 8, 2016, doi:10.3390/molecules21081105.
APA
Shang, C., Rougé, P., & Van Damme, E. (2016). Ribosome inactivating proteins from Rosaceae. MOLECULES, 21(8). https://doi.org/10.3390/molecules21081105
Chicago author-date
Shang, Chenjing, Pierre Rougé, and Els Van Damme. 2016. “Ribosome Inactivating Proteins from Rosaceae.” MOLECULES 21 (8). https://doi.org/10.3390/molecules21081105.
Chicago author-date (all authors)
Shang, Chenjing, Pierre Rougé, and Els Van Damme. 2016. “Ribosome Inactivating Proteins from Rosaceae.” MOLECULES 21 (8). doi:10.3390/molecules21081105.
Vancouver
1.
Shang C, Rougé P, Van Damme E. Ribosome inactivating proteins from Rosaceae. MOLECULES. 2016;21(8).
IEEE
[1]
C. Shang, P. Rougé, and E. Van Damme, “Ribosome inactivating proteins from Rosaceae,” MOLECULES, vol. 21, no. 8, 2016.
@article{8524331,
  abstract     = {{Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry. All RIP domains from Rosaceae share high sequence similarity with conserved residues in the catalytic site and the carbohydrate binding sites. The genomes of Malus domestica and Pyrus communis contain both type 1 and type 2 RIP sequences, whereas for Prunus mume, Prunus persica, Pyrus bretschneideri, and Pyrus communis a complex set of type 1 RIP sequences was retrieved. Heterologous expression and purification of the type 1 as well as the type 2 RIP from apple allowed to characterize the biological activity of the proteins. Both RIPs from Malus domestica can inhibit protein synthesis. Furthermore, molecular modelling suggests that RIPs from Rosaceae possess three-dimensional structures that are highly similar to the model proteins and can bind to RIP substrates. Screening of the recombinant type 2 RIP from apple on a glycan array revealed that this type 2 RIP interacts with terminal sialic acid residues. Our data suggest that the RIPs from Rosaceae are biologically active proteins.}},
  articleno    = {{1105}},
  author       = {{Shang, Chenjing and Rougé, Pierre and Van Damme, Els}},
  issn         = {{1420-3049}},
  journal      = {{MOLECULES}},
  keywords     = {{carbohydrate binding activity,molecular modeling,protein synthesis inhibition,ribosome-inactivating proteins,RICIN-A-CHAIN,ELDERBERRY SAMBUCUS-NIGRA,PLANTA ANTIVIRAL ACTIVITY,ACTIVE-SITE,MOMORDICA-CHARANTIA,TRANSGENIC TOBACCO,CRYSTAL-STRUCTURE,SIALIC-ACID,IRIS BULBS,IN-VIVO}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{17}},
  title        = {{Ribosome inactivating proteins from Rosaceae}},
  url          = {{http://doi.org/10.3390/molecules21081105}},
  volume       = {{21}},
  year         = {{2016}},
}

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