Targeting ricin to the ribosome.
作者： Kerrie L. May , Qing Yan , Nilgun E. Tumer
DOI: 10.1016/J.TOXICON.2013.02.001
关键词:
摘要: Abstract The plant toxin ricin is highly toxic for mammalian cells and of concern bioterrorism. Ricin belongs to a family functionally related toxins, collectively referred as ribosome inactivating proteins (RIPs), which disable ribosomes halt protein synthesis. Currently there are no specific antidotes against or RIPs. catalytic subunit an N-glycosidase that depurinates universally conserved adenine residue within the sarcin/ricin loop (SRL) 28S rRNA. This depurination activity inhibits translation its biochemistry has been intensively studied. Yet, recent developments paint more complex picture toxicity, with ribosomal cellular signaling pathways contributing potency ricin. In particular, several studies have now established importance stalk structure in facilitating specificity other review highlights defining toxin–ribosome interactions examines significance these toxicity therapeutic intervention.
sci-hub.se 参考文章(105)
E. Honjo, K. Watanabe, T. Tsukamoto, Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation. Journal of Biochemistry. ,vol. 131, pp. 267- 275 ,(2002) , 10.1093/OXFORDJOURNALS.JBCHEM.A003098
Jennifer S. Gray, Hee Kyong Bae, James C. B. Li, Allan S. Lau, James J. Pestka, Double-stranded RNA-activated protein kinase mediates induction of interleukin-8 expression by deoxynivalenol, Shiga toxin 1, and ricin in monocytes. Toxicological Sciences. ,vol. 105, pp. 322- 330 ,(2008) , 10.1093/TOXSCI/KFN128
J. Michael Lord, Lynne M. Roberts, Toxin Entry: Retrograde Transport through the Secretory Pathway Journal of Cell Biology. ,vol. 140, pp. 733- 736 ,(1998) , 10.1083/JCB.140.4.733
Jia-Chi Chiou, Xiao-Ping Li, Miguel Remacha, Juan P.G. Ballesta, Nilgun E. Tumer, Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2 The International Journal of Biochemistry & Cell Biology. ,vol. 43, pp. 1792- 1801 ,(2011) , 10.1016/J.BIOCEL.2011.08.018
Heather P Harding, Isabel Novoa, Yuhong Zhang, Huiqing Zeng, Ron Wek, Matthieu Schapira, David Ron, Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells Molecular Cell. ,vol. 6, pp. 1099- 1108 ,(2000) , 10.1016/S1097-2765(00)00108-8
Robert A. SPOONER, Peter D. WATSON, Catherine J. MARSDEN, Daniel C. SMITH, Katherine A. H. MOORE, Jonathon P. COOK, J. Michael LORD, Lynne M. ROBERTS, Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum. Biochemical Journal. ,vol. 383, pp. 285- 293 ,(2004) , 10.1042/BJ20040742
Kotlo U. Kumar, Sri P. Srivastava, Randal J. Kaufman, Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18 Molecular and Cellular Biology. ,vol. 19, pp. 1116- 1125 ,(1999) , 10.1128/MCB.19.2.1116
Alexandra Stolz, Dieter H. Wolf, Endoplasmic reticulum associated protein degradation: A chaperone assisted journey to hell Biochimica et Biophysica Acta. ,vol. 1803, pp. 694- 705 ,(2010) , 10.1016/J.BBAMCR.2010.02.005
Mihaela Diaconu, Ute Kothe, Frank Schlünzen, Niels Fischer, Jörg M. Harms, Alexander G. Tonevitsky, Holger Stark, Marina V. Rodnina, Markus C. Wahl, Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation Cell. ,vol. 121, pp. 991- 1004 ,(2005) , 10.1016/J.CELL.2005.04.015
Deyi Qiu, Pilar Parada, Alberto García Marcos, David Cárdenas, Miguel Remacha, Juan P. G. Ballesta, Different roles of P1 and P2 Saccharomyces cerevisiae ribosomal stalk proteins revealed by cross-linking. Molecular Microbiology. ,vol. 62, pp. 1191- 1202 ,(2006) , 10.1111/J.1365-2958.2006.05445.X