Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3′ untranslated region

Molecular and Cellular Biology

Volumn 23, Issue 5, 2003, Pages 1509-1519

  Sampath, Prabha ^a,b   Mazumder, Barsanjit ^a   Seshadri, Vasudevan ^a   Fox, Paul L ^a,b  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CLEVELAND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CERULOPLASMIN; CIRCULAR DNA; CYTOKINE; GAMMA INTERFERON; INITIATION FACTOR 4G; MESSENGER RNA; POLYADENYLIC ACID; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN; PROTEIN GAIT; UNCLASSIFIED DRUG;

3' UNTRANSLATED REGION; ARTICLE; AUTORADIOGRAPHY; BASE PAIRING; BINDING AFFINITY; CONTROLLED STUDY; CYTOKINE PRODUCTION; DELETION MUTANT; EUKARYOTE; GENE EXPRESSION; GENE SILENCING; HUMAN; HUMAN CELL; INFLAMMATION; MOLECULAR MECHANICS; MONOCYTE; MUTATIONAL ANALYSIS; NUCLEIC ACID BASE SUBSTITUTION; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PHYLOGENY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; RNA STRUCTURE; RNA TRANSCRIPTION; TRANSLATION REGULATION;

3' UNTRANSLATED REGIONS; ALGORITHMS; BASE SEQUENCE; BINDING, COMPETITIVE; BLOTTING, NORTHERN; CERULOPLASMIN; CLONING, MOLECULAR; CYTOSOL; DOWN-REGULATION; GENE SILENCING; HUMANS; INTERFERON TYPE II; MODELS, GENETIC; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; PROTEIN BIOSYNTHESIS; RNA; RNA, COMPLEMENTARY; RNA, MESSENGER; TIME FACTORS; TRANSCRIPTION, GENETIC; U937 CELLS;

EUKARYOTA;

EID: 0037371348     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.5.1509-1519.2003     Document Type: Article

References (40)

1. Ben-Asouli, Y., Y. Banai, Y. Pel-Or, A. Shir, and R. Kaempfer. 2002. Human interferon-γ mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR. Cell 108:221-232.
2. Bielli, P., and L. Calabrese. 2002. Structure to function relationships in ceruloplasmin: a "moonlighting" protein. Cell. Mol. Life Sci. 59:1413-1427.
3. Cho, D. C., E. C. Scharl, and J. A. Steitz. 1995. Decreasing the distance between the two conserved sequence elements of histone premessenger RNA interferes with 3′ processing in vitro. RNA 1:905-914.
4. Conne, B., A. Stutz, and J. D. Vassalli. 2000. The 3′ untranslated region of messenger RNA: a molecular "hotspot" for pathology? Nat. Med. 6:637-641.
5. Deiss, L. P., E. Feinstein, H. Berissi, O. Cohen, and A. Kimchi. 1995. Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death. Genes Dev. 9:15-30.
6. Dominski, Z., and W. F. Marzluff. 1999. Formation of the 3′ end of histone mRNA. Gene 239:1-14,
7. Ehrenwald, E., G. M. Chisolm, and P. L. Fox. 1994. Intact human ceruloplasmin oxidatively modifies low density lipoprotein. J. Clin. Investig. 93:1493-1501.
8. Fletcher, J. E., P. R. Copeland, D. M. Driscoll, and A. Krol. 2001. The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2. RNA 7:1442-1453.
9. Harris, Z. L., A. P. Durley, T. K. Man, and J. D. Gitlin. 1999. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. USA 96:10812-10817.
10. Imataka, H., A. Gradi, and N. Sonenberg. 1998. A newly identified N- terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17:7480-7489.
11. Jaeger, J. A., D. H. Turner, and M. Zuker. 1989, Improved predictions of secondary structures for RNA. Proc. Natl. Acad. Sci. USA 86:7706-7710.
12. Kalmovarin, N., W. E. Friedrichs, H. V. O'Brien, L. A. Linehan, B. H. Bowman, and F. Yang. 1991. Extrahepatic expression of plasma protein genes during inflammation. Inflammation 15:369-379.
13. Katzenellenbogen, R. A., S. B. Baylin, and J. G. Herman. 1999. Hypermethylation of the DAP-kinase CpG island is a common alteration in B-cell malignancies. Blood 93:4347-4353.
14. Kirkpatrick, P. 2002. Putting the brake on inflammation. Nat. Rev. 1:99.
15. Klausner, R. D., T. A. Rouault, and J. B. Harford. 1993. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72:19-28.
16. 2+, ceruloplasmin, and phosphate. Arch. Biochem. Biophys. 295:302-308.
17. Lockhart, P. J., and J. F. Mercer. 1999. Cloning and expression analysis of the sheep ceruloplasmin cDNA. Gene 236:251-257.
18. Mazumder, B., and P. L. Fox. 1999. Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells: role of the 3′ untranslated region. Mol. Cell. Biol. 19:6898-6905.
19. Mazumder, B., C. K. Mukhopadhyay, A. Prok, M. K. Cathcart, and P. L. Fox. 1997. Induction of ceruloplasmin synthesis by IFN-γ in human monocytic cells. J. Immunol. 159:1938-1944.
20. Mazumder, B., V. Seshadri, and P. L. Fox. Translational control by the 3′-UTR: the ends specify the means. Trends Biochem. Sci., in press.
21. Mazumder, B., V. Seshadri, H. Imataka, N. Sonenberg, and P. L. Fox. 2001. Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4G. Mol. Cell. Biol. 21:6440-6449.
22. McDonald, P. P., V. A. Fadok, D. Bratton, and P. M. Henson. 1999. Transcriptional and translational regulation of inflammatory mediator production by endogenous TGF-β in macrophages that have ingested apoptotic cells. J. Immunol. 163:6164-6172.
23. Mendell, J. T., and H. C. Dietz. 2001. When the message goes awry: disease- producing mutations that influence mRNA content and performance. Cell 107:411-414.
24. Mezzetti, A., M. D. Guglielmi, S. D. Pierdomenico, F. Costantini, F. Cipollone, D. De Cesare, T. Bucciarelli, S. Ucchino, F. Chiarelli, F. Cuccurullo, and F. Romano. 1999. Increased systemic oxidative stress after elective endarterectomy: relation to vascular healing and remodeling. Arterioscler. Thromb. Vasc. Biol. 19:2659-2665.
25. Mukhopadhyay, C. K., and P. L. Fox. 1998. Ceruloplasmin copper induces oxidant damage by a redox process utilizing cell-derived superoxide as reductant. Biochemistry 37:14222-14229.
26. Mukhopadhyay, C. K., B. Mazumder, P. F. Lindley, and P. L. Fox. 1997. Identification of the prooxidant site of human ceruloplasmin: a model for oxidative damage by copper bound to protein surfaces. Proc. Natl. Acad. Sci. USA 94:11546-11551.
27. Osaki, S., D. A. Johnson, and E. Frieden. 1966. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241:2746-2751.
28. Ostareck, D. H., A. Ostareck-Lederer, M. Wilm, B. J. Thiele, M. Mann, and M. W. Hentze. 1997. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89:597-606.
29. Pesole, G., S. Liuni, and M. D'Souza. 2000. PatSearch: a pattern matcher software that finds functional elements in nucleotide and protein sequences and assesses their statistical significance. Bioinformatics 16:439-450.
30. Pesole, G., S. Liuni, G. Grillo, F. Licciulli, F. Mignone, C. Gissi, and C. Saccone. 2002. UTRdb and UTRsite: specialized databases of sequences and functional elements of 5′ and 3′ untranslated regions of eukaryotic mRNAs. Update 2002. Nucleic Acids Res. 30:335-340.
31. Piecyk, M., S. Wax, A. R. Beck, N. Kedersha, M. Gupta, B. Maritim, S. Chen, C. Gueydan, V. Kruys, M. Streuli, and P. Anderson. 2000. TIA-1 is a translational silencer that selectively regulates the expression of TNF-α. EMBO J. 19:4154-4163.
32. Preiss, T., and M. W. Hentze. 1999. From factor to mechanisms: translation and translational control in eukaryotes. Curr. Opin. Genet. Dev. 9:515-521.
33. Rydén, L. 1984. Ceruloplasmin, p. 37-100. In R. Lontie (ed.), Copper proteins and copper enzymes, vol. III. CRC Press, Boca Raton, Fla.
34. Sachs, A. B., and G. Varani. 2000. Eukaryotic translation initiation: there are (at least) two sides to every story. Nat. Struct. Biol. 7:356-361.
35. Saenko, E. L., O. V. Skorobogat'ko, P. Tarasenko, V. Romashko, L. Zhuravetz, L. Zadorozhnaya, O. F. Senjuk, and A. I. Yaropolov. 1994. Modulatory effects of ceruloplasmin on lymphocytes, neutrophils and monocytes of patients with altered immune status. Immunol. Investig. 23:99-114.
36. Salonen, J. T., R. Salonen, K. Seppänen, M. Kantola, S. Suntioinen, and H. Korpela. 1991. Interactions of serum copper, selenium, and low density lipoprotein cholesterol in atherogenesis. Br. Med. J. 302:756-760.
37. Suh, Y. A., R. S. Arnold, B. Lassegue, J. Shi, X. Xu, D. Sorescu, A. B. Chung, K. K. Griendling, and J. D. Lambeth. 1999. Cell transformation by the superoxide-generating oxidase Mox1. Nature 401:79-82.
38. Thompson, J. F., L. S. Hayes, and D. B. Lloyd. 1991. Modulation of firefly luciferase stability and impact on studies of gene regulation. Gene 103:171-177.
39. Van Lenten, B. J., S. Y. Hama, F. C. De Beer, D. M. Stafforini, T. M. McIntyre, S. M. Prescott, B. N. La Du, A. M. Fogelman, and M. Navab. 1995. Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures. J. Clin. Investig. 96:2758-2767.
40. Yoshida, K., K. Furihata, S. Takeda, A. Nakamura, K. Yamamoto, H. Morita, S. Hiyamuta, S. Ikeda, N. Shimizu, and N. Yanagisawa. 1995. A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat. Genet. 9:267-272.