The trichomonad cysteine proteinase TVCP4 transcript contains an iron-responsive element

FEBS Letters

Volumn 581, Issue 16, 2007, Pages 2919-2928

  Solano González, Eduardo ^a   Burrola Barraza, Eduviges ^a   León Sicairos, Claudia ^a   Avila González, Leticia ^a   Gutiérrez Escolano, Lorena ^a   Ortega López, Jaime ^a   Arroyo, Rossana ^a  

^a DEPARTAMENTO DE FÍSICA   (Mexico)

Author keywords

Cysteine proteinases; Iron regulation; Iron responsive element iron regulatory protein system; Iron responsive elements; Post transcriptional regulation; RNA binding proteins; Trichomonas vaginalis

Indexed keywords

CYSTEINE PROTEINASE; CYTOPLASM PROTEIN; FERRITIN; IRON BINDING PROTEIN; IRON REGULATORY PROTEIN 1; MESSENGER RNA;

5' UNTRANSLATED REGION; ARTICLE; CONTROLLED STUDY; CROSS LINKING; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; IRON BINDING CAPACITY; IRON RESPONSIVE ELEMENT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; TRICHOMONAS VAGINALIS; ULTRAVIOLET RADIATION;

ANIMALS; BASE SEQUENCE; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; ENZYME PRECURSORS; HELA CELLS; HUMANS; IRON; IRON REGULATORY PROTEIN 1; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; RECOMBINANT PROTEINS; RESPONSE ELEMENTS; RNA, MESSENGER; RNA-BINDING PROTEINS; TRICHOMONAS VAGINALIS;

TRICHOMONADIDA; TRICHOMONAS VAGINALIS;

EID: 34250339684     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.056     Document Type: Article

References (45)

1. Wilson M.E., and Britigan B.E. Iron acquisition by parasitic protozoa. Parasitol. Today 14 (1998) 348-353
2. Gorrell T.E. Effects of culture medium content on the biochemical composition and metabolism of Trichomonas vaginalis. J. Bacteriol. 161 (1985) 1228-1230
3. De Jesus J.B., Ferreira M.A., Cuervo P., Britto C., Silva-Filho F.C., and Meyer-Fernandes J.R. Iron modulates ecto-phosphohydrolase activities in pathogenic trichomonads. Parasitol. Int. 55 (2006) 285-290
4. Lehker M.W., Arroyo R., and Alderete J.F. The regulation by iron of the synthesis of adhesins and cytoadherence levels in the protozoan Trichomonas vaginalis. J. Exp. Med. 174 (1991) 311-318
5. Arroyo R., Engbring J., Nguyen J., Musatovova O., Lopez O., Lauriano C., and Alderete J.F. Characterization of cDNAs encoding adhesin proteins involved in Trichomonas vaginalis cytoadherence. Arch. Med. Res. 26 (1995) 361-369
6. Garcia A., Chang T., Benchimol M., Klumpp D., Lehker M., and Alderete J.F. Iron and contact with host cells induce expression of adhesins on surface of Trichomonas vaginalis. Mol. Microbiol. 47 (2003) 1207-1224
7. Moreno-Brito V., Yañez-Gómez C., Meza-Cervántez P., Avila-González L., Rodri{dotless}́guez-Rodri{dotless}́guez M.A., Ortega-López J., González-Robles A., and Arroyo R. A Trichomonas vaginalis 120-kDa protein with identity to hydrogenosome pyruvate ferredoxin oxidorreductase is a surface adhesin induced by iron. Cell. Microbiol. 7 (2005) 245-258
8. Alderete J.F., Provenzano D., and Lehker M.W. Iron mediates Trichomonas vaginalis resistance to complement lysis. Microb. Pathogen. 19 (1995) 93-103
9. Crouch M.L., and Alderete J.F. Trichomonas vaginalis has two fibronectin-like iron-regulated genes. Arch. Med. Res. 32 (2001) 102-107
10. León-Sicairos C.R., León-Félix J., and Arroyo R. Tvcp12: a novel Trichomonas vaginalis cathepsin L-like cysteine proteinase-encoding gene. Microbiology (UK) 150 (2004) 1131-1138
11. Tsai C.D., Liu H.W., and Tai J.H. Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis. J. Biol. Chem. 277 (2002) 5153-5162
12. Ong S.J., Huang S.C., Liu H.W., and Tai J.S. Involvement of multiple DNA elements in iron-inducible transcription of the ap65-1 gene in the protozoan parasite Trichomonas vaginalis. Mol. Microbiol. 52 (2004) 1721-1730
13. Ong S.J., Hsu H.M., Liu H.W., Chu C.H., and Tai J.H. Activation of multifarious transcription of an adhesion protein ap65-1 gene by a novel Myb2 protein in the protozoan parasite Trichomonas vaginalis. J. Biol. Chem. 282 (2007) 6716-6725
14. Testa U. Iron-responsive elements and iron regulatory proteins. In: Testa U. (Ed). Proteins of Iron Metabolism (2002), CRC Press, Boca Raton, FL, USA 407-448
15. Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system. Ann. N. Y. Acad. Sci. 1012 (2004) 1-13
16. Hentze M.W., Muckenthaler M.U., and Andrews N.C. Balancing acts: molecular control of mammalian iron metabolism. Cell 117 (2004) 285-297
17. Rouault T.A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2 (2006) 406-414
18. Neale K.A., and Alderete J.F. Analysis of the proteinases of representative Trichomonas vaginalis isolates. Infect. Immun. 58 (1990) 157-162
19. Arroyo R., and Alderete J.F. Trichomonas vaginalis surface proteinase activity is necessary for parasite adherence to epithelial cells. Infect. Immun. 57 (1989) 2991-2997
20. Mendoza-López R., Becerril-Garci{dotless}́a C., Fattel-Facenda L.V., Avila- González L., Ruiz-Tachiqui{dotless}́n M., Ortega-López J., and Arroyo R. CP30, a cysteine proteinase involved in Trichomonas vaginalis cytoadherence. Infect. Immun. 68 (2000) 4907-4912
21. Hernandez H., Sariego I., Garber G., Delgado R., Lopez O., and Sarracent J. Monoclonal antibodies against a 62 kDa proteinase of Trichomonas vaginalis decrease parasites cytoadherence to epithelial cells and confer protection to mice. Parasite Immunol. 26 (2004) 119-125
22. Alvarez-Sánchez M.E., Avila-González L., Becerril-Garci{dotless}́a C., Fattel-Facenda L.V., and Arroyo R. A novel cysteine proteinase (CP65) of Trichomonas vaginalis involved in cytotoxicity. Microb. Pathog. 28 (2000) 193-202
23. Hernández-Gutiérrez R., Avila-González L., Ortega-López J., Cruz-Talonia F., Gómez-Gutiérrez G., and Arroyo R. Trichomonas vaginalis: characterization of a 39-kDa cysteine proteinase found in patient vaginal secretions. Exp. Parasitol. 107 (2004) 125-135
24. Diamond L. The establishment of various trichomonads of animals and men in axenic culture. J. Parasitol. 43 (1957) 488-490
25. Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31 (2003) 3406-3415
26. Alderete J.F. Antigenic analysis of several pathogenic strains of Trichomonas vaginalis. Infect. Immun. 39 (1983) 1041-1047
27. Kaldy P., Menotti E., Moret R., and Kühn L.C. Identification of RNA-binding surfaces in iron regulatory protein-1. EMBO J. 18 (1999) 6073-6083
28. Henderson B.R., Menotti E., Bonard C., and Kühn L.C. Optimal sequence and structure of iron-responsive elements. Selection of RNA-stem-loops with high affinity for iron regulatory factor. J. Biol. Chem. 269 (1994) 17481-17489
29. Henderson B.R., Menotti E., and Kühn L.C. Iron regulatory proteins 1 and 2 bind distinct sets of RNA target sequences. J. Biol. Chem. 271 (1996) 4900-4908
30. Harlow D., and Lane E. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory, New York, USA
31. Campbell K.S., Bedzyk W.D., and Cambier J.C. Manipulation of B cell antigen receptor tyrosine phosphorylation using aluminum fluoride and sodium orthovanadate. Mol. Immunol. 32 (1995) 1283-1294
32. Gutierrez-Escolano L., Vazquez-Ochoa M., Escobar-Herrera J., and Hernandez-Acosta J. La, PTB, and PAB proteins bind to the 3′ untranslated region of Norwalk virus genomic RNA. Biochem. Biophys. Res. Commun. 311 (2003) 759-766
33. Liston D.R., and Johnson P.J. Analysis of a ubiquitous promoter element in a primitive eukaryote: early evolution of the initiator element. Mol. Cell. Biol. 19 (1999) 2380-2388
34. Espinosa N., Hernández R., López-Griego L., Arroyo R., and López-Villaseñor I. Differences between coding and non-coding regions in the Trichomonas vaginalis genome: an actin gene as a locus model. Acta Trop. 78 (2001) 147-154
35. Mallinson D.J., Lockwood B.C., Coombs G.H., and North M. Identification and molecular cloning of four cysteine proteinase genes from the pathogenic protozoan Trichomonas vaginalis. Microbiology 140 (1994) 2725-2735
36. Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., et al. Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis. Science 315 (2007) 207-212
37. Addess K.J., Basilion J.P., Klausner R.D., Rouault T.A., and Pardi A.J. Structure and dynamics of the iron responsive element RNA: implications for binding of the RNA by iron regulatory proteins. J. Mol. Biol. 274 (1997) 72-83
38. Lin E., Graziano J.H., and Freyer G.A. Regulation of the 75-kDa subunit of mitochondrial complex I by iron. J. Biol. Chem. 276 (2001) 27685-27692
39. Paraskeva E., Gray N.K., Schläger B., Wehr K., and Hentze M.W. Ribosomal pausing and scanning arrest as mechanisms of translational regulation from cap-distal iron-responsive elements. Mol. Cell. Biol. 19 (1999) 807-816
40. Koloteva N., Mueller P.P., and McCarthy J.E.G. The position dependence of translational regulation via RNA-RNA and RNA-protein interactions in the 5′-untranslated region. J. Biol. Chem. 271 (1997) 16531-16539
41. Loyevsky M., Mompoint F., Yikilmaz E., Altschul S.F., Madden T., Wootton J.C., Kurantsin-Mills J., Kassim O.O., Gordeuk V.R., and Rouault T.A. Expression of a recombinant IRP-like Plasmodium falciparum protein that specifically binds putative plasmodial IREs. Mol. Biochem. Parasitol. 126 (2003) 231-238
42. Serio A.W., Pechter K.B., and Sonenshein A.L. Bacillus subtilis aconitase is required for efficient late-sporulation gene expression. J. Bacteriol. 188 (2006) 6396-6405
43. Rogers J.T., Randall J.D., Cahill C.M., Eder P.S., Huang X., Gunshin H., Leiter L., McPhee J., Sarang S.S., Utsuki T., Greig N.H., Lahiri D.K., Tanzi R.E., Bush A.I., Giordano T., and Gullans S.R. An iron-responsive element type II in the 5′-untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277 (2002) 45518-45528
44. Kohler S.A., Henderson B.R., and Kühn L.C. Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region. J. Biol. Chem. 270 (1995) 30781-30786
45. Kim H.Y., LaVaute T., Iwai K., Klausner R.D., and Rouault T.A. Identification of a conserved and functional iron-responsive element in the 5′-untranslated region of mammalian mitochondrial aconitase. J. Biol. Chem. 271 (1996) 24226-24230