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Chapter 17 : Plant and Bacterial Toxins as RNA -Glycosidases

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Plant and Bacterial Toxins as RNA -Glycosidases, Page 1 of 2

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Abstract:

Along with identification of the enzymatic function of ribosome-inactivating proteins (RIPs) came the recognition that certain bacterial toxins, called Shiga toxins (Stxs), fit into the category of plant proteins. We now know that these plant and bacterial poisons have the broader specificity of polynucleotide:adenosine glycosidases, at least in vitro. This chapter refers to the enzymes interchangeably as RIPs or RNA -glycosidases. Recently, additional enzymatic activities have been attributed to the RIPs. However, when four different RIPs were highly purified, the only enzymatic activity they retained was the capacity to remove adenine from rRNA or DNA. This observation indicates that the RIPs, originally defined as RNA -glycosidases, are actually polynucleotide:adenosine glycosidases, at least in vitro. One unusual feature of the RIPs is that, although they share the same enzymatic activity and their preferred target is intact mammalian ribosomes, they are not equally active on target ribosomes in vitro. There appear to be at least two explanations for this phenomenon. One reason that some RNA -glycosidases do not appear to be as active as others in cell-free assays is that they require cofactors such as ATP. The second reason that some RIPs have varying specificities is that they appear to interact with ribosomal proteins. Consistent with a protective function for the plant RNA -glycosidases is that the RIPs are both lethal and often stored in large quantities.

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17

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Figures

Image of Figure 1
Figure 1

Schematic of a portion of the S/R loop in 28S rRNA that serves as the substrate for the RIPs. The RIP catalyzes release of the adenine residue from the loop without cleavage of the sugar backbone (shown as open circles) of the rRNA.

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17
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Image of Figure 2
Figure 2

Crystal structures of the (A) type 1 RIP bryodin 1 (Protein Data Bank [PDB] ID: 1BRY, Gawlak et al. [ ]) and the type 2 RIPs (B) ricin (PDB ID: 2AAI, Rutenber et al. [ ]) and (C) Stx (PDB ID: 1DMO, Fraser et al. [ ]).

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17
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Image of Figure 3
Figure 3

Potential to protect autologous ribosomes from the plant's own RIP. (i) The RIP is produced in an inactive form. (ii) The RIP is active but stored so that it does not have access to the ribosome. (iii) The ribosome is refractory to the action of the RIP. (iv) The RIP requires a cofactor that is absent in the cytosol. (v) The active site of the enzyme is blocked. (vi) The active RIP is secreted into the cell wall or outside the cell.

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17
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References

/content/book/10.1128/9781555817893.chap17
1. Barbieri, L.,, P. Valbonesi,, F. Righi,, G. Zuccheri,, F. Monti,, P. Gorini,, B. Samori,, and F. Stirpe. 2000. Polynucleotide:adenosine glycosidase is the sole activity of ribosomeinactivating proteins on DNA. J. Biochem. 128:883889.
2. Fraser, M. E.,, M. M. Chernaia,, Y. V. Kozlov,, and M. N. James. 1994. Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A° resolution. Nat. Struct. Biol. 1:5964.
3. Gawlak, S. L.,, M. Neubauer,, H. E. Klei,, C. Y. Chang,, H. M. Einspahr,, and C. B. Siegall. 1997. Molecular, biological, and preliminary structural analysis of recombinant bryodin 1, a ribosome-inactivating protein from the plant Bryonia dioica. Biochemistry 36:30953103.
4. Rutenber, E.,, B. J. Katzin,, S. Ernst,, E. J. Collins,, D. Mlsna,, M. P. Ready,, and J. D. Robertus. 1991. Crystallographic refinement of ricin to 2.5 A° . Proteins 10:240250.
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6. Melton-Celsa, A. R.,, J. E. Rogers,, C. K. Schmitt,, S. C. Darnell,, and A. D. O’Brien. 2001. Virulence of Shiga toxin-producing Escherichia coli (STEC) in orally-infected mice correlates with the type of toxin produced by the infecting strain. Jpn. J. Med. Sci. Biol. 50:S108S114.
7. Nielsen, K.,, and R. S. Boston. 2001. Ribosome-inactivating proteins: a plant perspective. Annu. Rev. Physiol. Plant Mol. Biol. 52:785816.
8. Paton, J. C.,, and A. W. Paton. 1998. Pathogenesis and diagnosis of Shiga toxinproducing Escherichia coli infections. Clin. Microbiol. Rev. 11:450479.
9. Peumans, W. J.,, Q. Hao,, and E. J. M. Van Damme. 2001. Ribosome-inactivating proteins from plants: more than RNA N-glycosidases? FASEB J. 15:14931506.
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Tables

Generic image for table
Table 1

Examples of type 1 RIPs

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17
Generic image for table
Table 2

Examples of type 2 RIPs

Citation: Melton-Celsa A, O'Brien A. 2003. Plant and Bacterial Toxins as RNA -Glycosidases, p 245-255. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch17

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