The biosynthesis and biological function of diphthamide

Critical Reviews in Biochemistry and Molecular Biology

Volumn 48, Issue 6, 2013, Pages 515-521

  Su, Xiaoyang ^a   Lin, Zhewang ^a   Lin, Hening ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

Diphthamide; Diphtheria toxin; Diphthine; Post translational modifications; Radical SAM enzyme

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYSTEINE; DIPHTHAMIDE; HEAT SHOCK PROTEIN 70; HISTIDINE DERIVATIVE; INTERLEUKIN 1BETA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; OXIDOREDUCTASE; RNA BINDING PROTEIN; RUBREDOXIN; UNCLASSIFIED DRUG; ZINC;

ADENOSINE DIPHOSPHATE RIBOSYLATION; AMIDATION; ARCHAEAL GENOME; BIOLOGICAL ACTIVITY; BIOSYNTHESIS; CELL FUNCTION; CHEMICAL STRUCTURE; CHIRALITY; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENDOCYTOSIS; ENDOSOME; ESCHERICHIA COLI; FAST ATOM BOMBARDMENT MASS SPECTROMETRY; G1 PHASE CELL CYCLE CHECKPOINT; GENE DELETION; GENE FUNCTION; GENE IDENTIFICATION; GENETIC CONSERVATION; GENETIC SCREENING; IN VITRO STUDY; METHYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; PYROCOCCUS HORIKOSHII; REGULATORY MECHANISM; REVIEW; SACCHAROMYCES CEREVISIAE; SECRETION (PROCESS); SPHEROPLAST; STEREOCHEMISTRY; TRANSCRIPTION REGULATION; X RAY CRYSTALLOGRAPHY;

ADP RIBOSE TRANSFERASES; ADP-RIBOSYLATION FACTORS; BACTERIAL TOXINS; DIPHTHERIA TOXIN; EXOTOXINS; HISTIDINE; PEPTIDE ELONGATION FACTOR 2; VIRULENCE FACTORS;

EID: 84888624530     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2013.831023     Document Type: Review

References (56)

1. Abdel-Fattah W, Scheidt V, Uthman S, et al. (2013). Insights into diphthamide, key diphtheria toxin effector. Toxins (Basel) 5:958-68.
2. Bar C, Zabel R, Liu S, et al. (2008). A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: kti11/Dph3. Mol Microbiol 69:1221-33.
3. Bektas M, Nurten R, Ergen K, Bermek E. (2006). Endogenous ADP-ribosylation for eukaryotic elongation factor 2: evidence of two different sites and reactions. Cell Biochem Function 24:369-80. (Pubitemid 44065242)
4. Bruening W, Prowse A, Schultz D, et al. (1999). Expression of OVCA1, a candidate tumor suppressor, is reduced in tumors and inhibits growth of ovarian cancer cells. Cancer Res 59:4973-83. (Pubitemid 29472903)
5. Carette J, Guimaraes C, Varadarajan M, et al. (2009). Haploid genetic screens in human cells identify host factors used by pathogens. Science 326:1231-5.
6. Chen CM, Behringer, RR. (2001). Cloning, structure, and expression of the mouse Ovca1 gene. Biochem Biophys Res Commun 286:1019-26. (Pubitemid 32924873)
7. Chen C-M, Behringer RR. (2004). Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis. Genes Dev 18:320-32. (Pubitemid 38199256)
8. Chen JY, Bodley JW. (1988). Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltrans-ferase. J Biol Chem 263:11692-6.
9. Chen J, Bodley JW, Livingston DM. (1985). Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae. Mol Cell Biol 5:3357-60. (Pubitemid 16233041)
10. Collier RJ. (2001). Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. Toxicon 39: 1793-803. (Pubitemid 32787010)
11. de Crecy-Lagard V, Forouhar F, Brochier-Armanet C, et al. (2012). Comparative genomic analysis of the DUF71/COG2102 family predicts roles in diphthamide biosynthesis and B12 salvage. Biol Direct 7:32.
12. Dunlop PC, Bodley JW. (1983). Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae. J Biol Chem 258:4754-8. (Pubitemid 13096364)
13. Elkins J, Podar M, Graham D, et al. (2008). A korarchaeal genome reveals insights into the evolution of the Archaea. Proc Natl Acad Sci USA 105:8102-7. (Pubitemid 351904715)
14. Fendrick J, Iglewski W, Moehring JM, Moehring TJ. (1992). Characterization of the endogenous ADP-ribosylation of wild-type and mutant elongation factor-II in eukaryotic cells. Eur J Biochem 205:25-31.
15. Fichtner L, Schaffrath R. (2002). KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44:865-75. (Pubitemid 34526595)
16. Frey P, Hegeman AD, Ruzicka FJ. (2008). The radical SAM superfamily. Crit Rev Biochem Mol Biol 43:63-88. (Pubitemid 351315858)
17. Greenwood C, Selth L, Dirac-Svejstrup AB, Svejstrup, JQ. (2009). An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator. J Biol Chem 284:141-9.
18. Honjo T, Nishizuka Y, Hayaishi O. (1968). Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis. J Biol Chem 243:3553-5.
19. Iglewski W, Lee H, Muller P. (1984). ADP-ribosyltransferase from beef liver which ADP-ribosylates elongation factor-2. FEBS Lett 173: 113-18.
20. Jager D, Werdan K, Muller-Werdan U. (2011). Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1beta. Mol Cell Biochem 348:125-8.
21. Jorgensen R, Merrill AR, Andersen GR. (2006). The life and death of translation elongation factor 2. Biochem Soc Trans 34:1-6. (Pubitemid 43239538)
22. Jorgensen R, Purdy A, Fieldhouse R, et al. (2008b). Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae. J Biol Chem 283: 10671-8.
23. Jorgensen R, Wang Y, Visschedyk D, Merrill AR. (2008a). The nature and character of the transition state for the ADP-ribosyltransferase reaction. EMBO Rep 9:802-9.
24. Jorgensen R, Yates S, Teal D, et al. (2004). Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae. J Biol Chem 279:45919-25. (Pubitemid 39491584)
25. Kong F, Tong R, Jia L, et al. (2011). OVCA1 inhibits the proliferation of epithelial ovarian cancer cells by decreasing cyclin D1 and increasing p16. Mol Cell Biochem 354:199-205.
26. Krogan N, Cagney G, Yu H, et al. (2006). Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440: 637-43.
27. Lee H, Iglewski WJ. (1984). Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A. Proc Natl Acad Sci USA 81:2703-7. (Pubitemid 14109327)
28. Lin H. (2011). S-Adenosylmethionine-dependent alkylation reactions: when are radical reactions used? Bioorg Chem 39:161-70.
29. Liu S, Bachran C, Gupta P, et al. (2012). Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development. Proc Natl Acad Sci USA 109: 13817-22.
30. Liu S, Milne G, Kuremsky J, et al. (2004). Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24:9487-97. (Pubitemid 39391685)
31. Liu S, Wiggins J, Sreenath T, et al. (2006). Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Mol Cell Biol 26:3835-41. (Pubitemid 43726400)
32. Mattheakis L, Shen W, Collier R. (1992). DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol 12:4026-37.
33. Moehring T, Danley DE, Moehring JM. (1984). In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin. Mol Cell Biol 4:642-50. (Pubitemid 14130360)
34. Ortiz P, Ulloque R, Kihara G, et al. (2006). Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance. J Biol Chem 281:32639-48. (Pubitemid 46036819)
35. Pappenheimer Jr A, Dunlop P, Adolph KW, Bodley JW. (1983). Occurrence of diphthamide in archaebacteria. J Bacteriol 153:1342-7. (Pubitemid 13126618)
36. Phillips N, Ziegler MR, Deaven LL. (1996a). A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3. Cancer Lett 102:85-90. (Pubitemid 26097807)
37. Phillips N, Ziegler M, Radford D, et al. (1996b). Allelic deletion on chromosome 17p13.3 in early ovarian cancer. Cancer Res 56:606-11. (Pubitemid 26043661)
38. Proudfoot M, Sanders S, Singer A, et al. (2008). Biochemical and structural characterization of a novel family of cystathionine [beta]-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375:301-15. (Pubitemid 350167436)
39. Robinson E, Henriksen O, Maxwell ES. (1974). Elongation factor 2. Amino acid sequence at the site of adenosine diphosphate ribosyla-tion. J Biol Chem 249:5088-93.
40. Sahi C, Craig EA. (2007). Network of general and specialty J protein chaperones of the yeast cytosol. Proc Natl Acad Sci USA 104: 7163-8. (Pubitemid 47186026)
41. Shi Y, Stefan C, Rue S, et al. (2011). Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway. Mol Biol Cell 22:4093-107.
42. Sjolinder M, Uhlmann J, Ponstingl H. (2004). Characterisation of an evolutionary conserved protein interacting with the putative guanine nucleotide exchange factor DelGEF and modulating secretion. Exp Cell Res 294:68-76. (Pubitemid 38229781)
43. Spahn C, Gomez-Lorenzo M, Grassucci R, et al. (2004). Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J 23:1008-19. (Pubitemid 38436866)
44. Su X, Chen W, Lee W, et al. (2012a). YBR246W is required for the third step of diphthamide biosynthesis. J Am Chem Soc 134:773-6.
45. Su X, Lin Z, Chen W, et al. (2012b). Chemogenomic approach identified yeast YLR143W as diphthamide synthetase. Proc Natl Acad Sci USA 109:19983-7.
46. Sun J, Zhang J, Wu F, et al. (2005). Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module. Biochemistry 44:8801-9. (Pubitemid 40840445)
47. Thakur A, Chitoor B, Goswami A, et al. (2012). Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. J Biol Chem 287: 13194-205.
48. Uthman S, Bar C, Scheidt V, et al. (2013). The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction network. PLoS Genet 9: e1003334.
49. Van Ness B, Howard JB, Bodley JW. (1978). Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin-modified yeast elongation factor 2. J Biol Chem 253:8687-90. (Pubitemid 9104649)
50. Van Ness B, Howard JB, Bodley JW. (1980a). ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. J Biol Chem 255:10717-20.
51. Van Ness B, Howard JB, Bodley JW. (1980b). ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products. J Biol Chem 255:10710-16.
52. Webb T, Cross S, McKie L, et al. (2008). Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development. J Cell Sci 121:3140-5.
53. Wei H, Bera T, Wayne A, et al. (2013). A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene. J Biol Chem 288:12305-12.
54. Zhang Y, Zhu X, Torelli A, et al. (2010). Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature 465:891-6.
55. Zhu X, Dzikovski B, Su X, et al. (2011). Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. Mol BioSystems 7:74-81.
56. Zhu X, Kim J, Su X, Lin H. (2010). Reconstitution of diphthine synthase activity in vitro. Biochemistry 49:9649-57.