- About this Journal ·
- Abstracting and Indexing ·
- Advance Access ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
BioMed Research International
Volume 2014 (2014), Article ID 424767, 20 pages
α-Actinin TvACTN3 of Trichomonas vaginalis Is an RNA-Binding Protein That Could Participate in Its Posttranscriptional Iron Regulatory Mechanism
Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN (CINVESTAV-IPN), 07360 México, DF, Mexico
Received 9 September 2013; Accepted 24 November 2013; Published 2 March 2014
Academic Editor: Wanderley De Souza
Copyright © 2014 Jaeson Santos Calla-Choque et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- P. Aisen, C. Enns, and M. Wessling-Resnick, “Chemistry and biology of eukaryotic iron metabolism,” International Journal of Biochemistry and Cell Biology, vol. 33, no. 10, pp. 940–959, 2001.
- U. Testa, Proteins of Iron Metabolism, CRC Press, Boca Raton, FL, USA, 2000.
- K. Pantopoulos, “Iron metabolism and the IRE/IRP regulatory system: an update,” Annals of the New York Academy of Sciences, vol. 1012, pp. 1–13, 2004.
- T. Rouault and R. Klausner, “Regulation of iron metabolism in eukaryotes,” Current Topics in Cellular Regulation, vol. 35, pp. 1–19, 1997.
- A. M. Thomson, J. T. Rogers, and P. J. Leedman, “Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation,” International Journal of Biochemistry and Cell Biology, vol. 31, no. 10, pp. 1139–1152, 1999.
- J. Wang and K. Pantopoulos, “Regulation of cellular iron metabolism,” Biochemical Journal, vol. 434, no. 3, pp. 365–381, 2011.
- C. P. Anderson, M. Shen, R. S. Eisenstein, and E. A. Leibold, “Mammalian iron metabolism and its control by iron regulatory proteins,” Biochimica et Biophysica Acta, vol. 1823, pp. 1468–1483, 2012.
- M. C. Kennedy, L. Mende-Mueller, G. A. Blondin, and H. Beinert, “Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, pp. 11730–11734, 1992.
- T. A. Rouault, “The role of iron regulatory proteins in mammalian iron homeostasis and disease,” Nature Chemical Biology, vol. 2, no. 8, pp. 406–414, 2006.
- D. J. Haile, T. A. Rouault, J. B. Harford et al., “Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 24, pp. 11735–11739, 1992.
- E. Solano-González, E. Burrola-Barraza, C. León-Sicairos et al., “The trichomonad cysteine proteinase TVCP4 transcript contains an iron-responsive element,” FEBS Letters, vol. 581, no. 16, pp. 2919–2928, 2007.
- J. C. Torres-Romero and R. Arroyo, “Responsiveness of Trichomonas vaginalis to iron concentrations: evidence for a post-transcriptional iron regulation by an IRE/IRP-like system,” Infection, Genetics and Evolution, vol. 9, no. 6, pp. 1065–1074, 2009.
- C.-D. Tsai, H.-W. Liu, and J.-H. Tai, “Characterization of an iron-responsive promoter in the protozoan pathogen Trichomonas vaginalis,” The Journal of Biological Chemistry, vol. 277, no. 7, pp. 5153–5162, 2002.
- L. S. Diamond, “The establishment of various trichomonads of animals and man in axenic cultures,” Journal of Parasitology, vol. 43, pp. 488–490, 1957.
- M. E. Alvarez-Sánchez, E. Solano-González, C. Yañez-Gómez, and R. Arroyo, “Negative iron regulation of the CP65 cysteine proteinase cytotoxicity in Trichomonas vaginalis,” Microbes and Infection, vol. 9, no. 14-15, pp. 1597–1605, 2007.
- R. Arroyo, J. Engbring, and J. F. Alderete, “Molecular basis of host epithelial cell recognition by Trichomonas vaginalis,” Molecular Microbiology, vol. 6, no. 7, pp. 853–862, 1992.
- Z. Popovic and D. M. Templeton, “A Northwestern blotting approach for studying iron regulatory element-binding proteins,” Molecular and Cellular Biochemistry, vol. 268, no. 1-2, pp. 67–74, 2005.
- B. R. Henderson, E. Menotti, C. Bonnard, and L. C. Kuhn, “Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor,” The Journal of Biological Chemistry, vol. 269, no. 26, pp. 17481–17489, 1994.
- L. T. Timchenko, P. Iakova, A. L. Welm, Z.-J. Cai, and N. A. Timchenko, “Calreticulin interacts with C/EBPα and C/EBPβ mRNAs and represses translation of C/EBP proteins,” Molecular and Cellular Biology, vol. 22, no. 20, pp. 7242–7257, 2002.
- E. A. Leibold and H. N. Munro, “Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated region of ferritin heavy- and light-subunit mRNAs,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 7, pp. 2171–2175, 1988.
- E. E. Figueroa-Angulo, P. Estrella-Hernandez, H. Salgado-Lugo, et al., “Cellular and biochemical characterization of two closely related triosephosphate isomerases from Trichomonas vaginalis,” Parasitology, vol. 139, pp. 1729–1738, 2012.
- A. L. Gutiérrez-Escolano, M. Vázquez-Ochoa, J. Escobar-Herrera, and J. Hernández-Acosta, “La, PTB, and PAB proteins bind to the 3′ untranslated region of Norwalk virus genomic RNA,” Biochemical and Biophysical Research Communications, vol. 311, no. 3, pp. 759–766, 2003.
- P. Meza-Cervantez, A. González-Robles, R. E. Cárdenas-Guerra et al., “Pyruvate: Ferredoxin oxidoreductase (PFO) is a surface-associated cell-binding protein in Trichomonas vaginalis and is involved in trichomonal adherence to host cells,” Microbiology, vol. 157, no. 12, pp. 3469–3482, 2011.
- S. L. Zhao, C. Y. Liang, W. J. Zhang, X. C. Tang, and H. Y. Peng, “Mapping the RNA-binding domain on the DpCPV VP4,” Archives of Virology, vol. 151, no. 2, pp. 273–283, 2006.
- C. R. León-Sicairos, J. León-Félix, and R. Arroyo, “Tvcp12: a novel Trichomonas vaginalis cathepsin L-like cysteine proteinase-encoding gene,” Microbiology, vol. 150, no. 5, pp. 1131–1138, 2004.
- I. Letunic, T. Doerks, and P. Bork, “SMART 6: recent updates and new developments,” Nucleic Acids Research, vol. 37, no. 1, pp. D229–D232, 2009.
- J. Schultz, F. Milpetz, P. Bork, and C. P. Ponting, “SMART, a simple modular architecture research tool: identification of signaling domains,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 11, pp. 5857–5864, 1998.
- C. J. A. Sigrist, L. Cerutti, E. De Castro et al., “PROSITE, a protein domain database for functional characterization and annotation,” Nucleic Acids Research, vol. 38, no. 1, Article ID gkp885, pp. D161–D166, 2009.
- J. M. Carlton, R. P. Hirt, J. C. Silva et al., “Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis,” Science, vol. 315, no. 5809, pp. 207–212, 2007.
- D. R. Liston and P. J. Johnson, “Analysis of a ubiquitous promoter element in a primitive eukaryote: early evolution of the initiator element,” Molecular and Cellular Biology, vol. 19, no. 3, pp. 2380–2388, 1999.
- N. Espinosa, R. Hernández, L. López-Griego, and I. López-Villaseñor, “Separable putative polyadenylation and cleavage motifs in Trichomonas vaginalis mRNAs,” Gene, vol. 289, no. 1-2, pp. 81–86, 2002.
- P. B. Dallas, S. Pacchione, D. Wilsker, V. Bowrin, R. Kobayashi, and E. Moran, “The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity,” Molecular and Cellular Biology, vol. 20, no. 9, pp. 3137–3146, 2000.
- X. Dou, S. Limmer, and R. Kreutzer, “DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA,” Journal of Molecular Biology, vol. 305, no. 3, pp. 451–458, 2001.
- D. J. Kenan and J. D. Keene, “La gets its wings,” Nature Structural and Molecular Biology, vol. 11, no. 4, pp. 303–305, 2004.
- T. A. Edwards, S. E. Pyle, R. P. Wharton, and A. K. Aggarwal, “Structure of pumilio reveals similarity between RNA and peptide binding motifs,” Cell, vol. 105, no. 2, pp. 281–289, 2001.
- T. Glisovic, J. L. Bachorik, J. Yong, and G. Dreyfuss, “RNA-binding proteins and post-transcriptional gene regulation,” FEBS Letters, vol. 582, no. 14, pp. 1977–1986, 2008.
- B. M. Lunde, C. Moore, and G. Varani, “RNA-binding proteins: modular design for efficient function,” Nature Reviews Molecular Cell Biology, vol. 8, no. 6, pp. 479–490, 2007.
- M. F. García-Mayoral, D. Hollingworth, L. Masino et al., “The Structure of the C-Terminal KH Domains of KSRP Reveals a Noncanonical Motif Important for mRNA Degradation,” Structure, vol. 15, no. 4, pp. 485–498, 2007.
- E. E. Figueroa-Angulo, F. J. Rendon-Gandarilla, J. Puente-Rivera, et al., “The effects of environmental factors on the virulence of Trichomonas vaginalis,” Microbes and Infection, vol. 14, pp. 1411–1427, 2012.
- S.-J. Ong, H.-M. Hsu, H.-W. Liu, C.-H. Chu, and J.-H. Tai, “Multifarious transcriptional regulation of adhesion protein gene ap65-1 by a novel Myb1 protein in the protozoan parasite Trichomonas vaginalis,” Eukaryotic Cell, vol. 5, no. 2, pp. 391–399, 2006.
- S.-J. Ong, H.-M. Hsu, H.-W. Liu, C.-H. Chu, and J.-H. Tai, “Activation of multifarious transcription of an adhesion protein ap65-1 gene by a novel Myb2 protein in the protozoan parasite Trichomonas vaginalis,” The Journal of Biological Chemistry, vol. 282, no. 9, pp. 6716–6725, 2007.
- H.-M. Hsu, S.-J. Ong, M.-C. Lee, and J.-H. Tai, “Transcriptional regulation of an iron-inducible gene by differential and alternate promoter entries of multiple Myb proteins in the protozoan parasite Trichomonas vaginalis,” Eukaryotic Cell, vol. 8, no. 3, pp. 362–372, 2009.
- M. Muckenthaler, N. Gunkel, D. Frishman, A. Cyrklaff, P. Tomancak, and M. W. Hentze, “Iron-regulatory protein-1 (IRP-1) is highly conserved in two invertebrate species—characterization of IRP-1 homologues in Drosophila melanogaster and Caenorhabditis elegans,” European Journal of Biochemistry, vol. 254, no. 2, pp. 230–237, 1998.
- D. Zhang, G. Dimopoulos, A. Wolf, B. Miñana, F. C. Kafatos, and J. J. Winzerling, “Cloning and molecular characterization of two mosquito iron regulatory proteins,” Insect Biochemistry and Molecular Biology, vol. 32, no. 5, pp. 579–589, 2002.
- C. Alén and A. L. Sonenshein, “Bacillus subtilis aconitase is an RNA-binding protein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 18, pp. 10412–10417, 1999.
- S. Banerjee, A. K. Nandyala, P. Raviprasad, N. Ahmed, and S. E. Hasnain, “Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase,” Journal of Bacteriology, vol. 189, no. 11, pp. 4046–4052, 2007.
- Y. Tang and J. R. Guest, “Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases,” Microbiology, vol. 145, no. 11, pp. 3069–3079, 1999.
- M. F. Addis, P. Rappelli, G. Delogu, F. Carta, P. Cappuccinelli, and P. L. Fiori, “Cloning and molecular characterization of a cDNA clone coding for Trichomonas vaginalis alpha-actinin and intracellular localization of the protein,” Infection and Immunity, vol. 66, no. 10, pp. 4924–4931, 1998.
- A. S. Kucknoor, V. Mundodi, and J. F. Alderete, “Adherence to human vaginal epithelial cells signals for increased expression of Trichomonas vaginalis genes,” Infection and Immunity, vol. 73, no. 10, pp. 6472–6478, 2005.
- R. K. Meyer and U. Aebi, “Bundling of actin filaments by α-actinin depends on its molecular length,” Journal of Cell Biology, vol. 110, no. 6, pp. 2013–2024, 1990.
- J. D. Dixson, M. R. J. Forstner, and D. M. Garcia, “The α-actinin gene family: a revised classification,” Journal of Molecular Evolution, vol. 56, no. 1, pp. 1–10, 2003.
- B. Sjöblom, A. Salmazo, and K. Djinović-Carugo, “α-Actinin structure and regulation,” Cellular and Molecular Life Sciences, vol. 65, no. 17, pp. 2688–2701, 2008.
- L. Horvathova, L. Safarikova, M. Basler, et al., “Transcriptomic identification of iron-regulated and iron-independent gene copies within the heavily duplicated Trichomonas vaginalis genome,” Genome Biology and Evolution, vol. 4, pp. 1017–1029, 2012.
- R.-P. Jansen, “RNA—cytoskeletal associations,” The FASEB Journal, vol. 13, no. 3, pp. 455–466, 1999.
- A. Vedeler, H. Hollas, A. K. Grindheim, and A. M. Raddum, “Multiple roles of annexin A2 in post-transcriptional regulation of gene expression,” Current Protein & Peptide Science, vol. 13, pp. 401–412, 2012.
- P. M. MacDonald, “bicoid mRNA localization signal: phylogenetic conservation of function and RNA secondary structure,” Development, vol. 110, no. 1, pp. 161–171, 1990.
- A. F. Ross, Y. Oleynikov, E. H. Kislauskis, K. L. Taneja, and R. H. Singer, “Characterization of a β-actin mRNA zipcode-binding protein,” Molecular and Cellular Biology, vol. 17, no. 4, pp. 2158–2165, 1997.