Ribosome Inactivating Proteins from Rosaceae
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, peac...
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| Format: | Article |
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MDPI AG
2016-08-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/21/8/1105 |
| _version_ | 1811310869548630016 |
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| author | Chenjing Shang Pierre Rougé Els J. M. Van Damme |
| author_facet | Chenjing Shang Pierre Rougé Els J. M. Van Damme |
| author_sort | Chenjing Shang |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T10:06:38Z |
| format | Article |
| id | doaj.art-c4375a033e0a49a6bf3ba51fb1917b81 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-04-13T10:06:38Z |
| publishDate | 2016-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-c4375a033e0a49a6bf3ba51fb1917b812022-12-22T02:51:03ZengMDPI AGMolecules1420-30492016-08-01218110510.3390/molecules21081105molecules21081105Ribosome Inactivating Proteins from RosaceaeChenjing Shang0Pierre Rougé1Els J. M. Van Damme2Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, BelgiumUnité Mixte de Recherche 152 Pharma Développement, Institut de Recherche pour le Développement, Université Paul Sabatier, 31062 Toulouse, FranceDepartment of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, BelgiumRibosome-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.http://www.mdpi.com/1420-3049/21/8/1105carbohydrate binding activitymolecular modelingprotein synthesis inhibitionribosome-inactivating proteins |
| spellingShingle | Chenjing Shang Pierre Rougé Els J. M. Van Damme Ribosome Inactivating Proteins from Rosaceae Molecules carbohydrate binding activity molecular modeling protein synthesis inhibition ribosome-inactivating proteins |
| title | Ribosome Inactivating Proteins from Rosaceae |
| title_full | Ribosome Inactivating Proteins from Rosaceae |
| title_fullStr | Ribosome Inactivating Proteins from Rosaceae |
| title_full_unstemmed | Ribosome Inactivating Proteins from Rosaceae |
| title_short | Ribosome Inactivating Proteins from Rosaceae |
| title_sort | ribosome inactivating proteins from rosaceae |
| topic | carbohydrate binding activity molecular modeling protein synthesis inhibition ribosome-inactivating proteins |
| url | http://www.mdpi.com/1420-3049/21/8/1105 |
| work_keys_str_mv | AT chenjingshang ribosomeinactivatingproteinsfromrosaceae AT pierrerouge ribosomeinactivatingproteinsfromrosaceae AT elsjmvandamme ribosomeinactivatingproteinsfromrosaceae |