메뉴 건너뛰기




Volumn 32, Issue 4, 2008, Pages 256-263

In silico analysis of EST and genomic sequences allowed the prediction of cis-regulatory elements for Entamoeba histolytica mRNA polyadenylation

Author keywords

Bioinformatics analysis; Cis regulatory elements; Pre mRNA 3 end processing; Protozoan parasite

Indexed keywords

CELLS; COMPUTATIONAL METHODS; NUCLEIC ACIDS; OPTICAL TOMOGRAPHY; RNA; TRANSCRIPTION;

EID: 45849136307     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2008.03.019     Document Type: Article
Times cited : (25)

References (42)
  • 3
    • 0027735142 scopus 로고
    • Unusual gene organization in the protozoan parasite Entamoeba histolytica
    • Bruchhaus M., Leippe C., Lioutas C., and Tannich E. Unusual gene organization in the protozoan parasite Entamoeba histolytica. DNA Cell Biol. 12 (1993) 925-933
    • (1993) DNA Cell Biol. , vol.12 , pp. 925-933
    • Bruchhaus, M.1    Leippe, C.2    Lioutas, C.3    Tannich, E.4
  • 4
    • 0029951973 scopus 로고    scopus 로고
    • Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica: molecular cloning, recombinant expression and inhibition by pyrophosphate analogues
    • Bruchhaus I., Jacobs T., Denart M., and Tannich E. Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica: molecular cloning, recombinant expression and inhibition by pyrophosphate analogues. Biochem. J. 316 (1996) 57-63
    • (1996) Biochem. J. , vol.316 , pp. 57-63
    • Bruchhaus, I.1    Jacobs, T.2    Denart, M.3    Tannich, E.4
  • 5
    • 4644263764 scopus 로고    scopus 로고
    • 3′ UTR signals necessary for expression of the Plasmodium gallinaceum ookinete protein, Pgs28, share similarities with those of yeast and plants
    • Cann H., Brown S.V., Oguariri R.M., and Golightly L.M. 3′ UTR signals necessary for expression of the Plasmodium gallinaceum ookinete protein, Pgs28, share similarities with those of yeast and plants. Mol. Biochem. Parasitol. 137 (2004) 239-245
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 239-245
    • Cann, H.1    Brown, S.V.2    Oguariri, R.M.3    Golightly, L.M.4
  • 6
    • 0032007547 scopus 로고    scopus 로고
    • Cloning and expression of the gene for the active PPi-dependent phosphofructokinase of Entamoeba histolytica
    • Deng Z., Huang M., Singh K., Albach R.A., Latshaw S.P., Chang K.P., and Kemp R.G. Cloning and expression of the gene for the active PPi-dependent phosphofructokinase of Entamoeba histolytica. Biochem. J. 329 (1998) 659-664
    • (1998) Biochem. J. , vol.329 , pp. 659-664
    • Deng, Z.1    Huang, M.2    Singh, K.3    Albach, R.A.4    Latshaw, S.P.5    Chang, K.P.6    Kemp, R.G.7
  • 7
    • 0037735612 scopus 로고
    • Genomic and cDNA actin sequences from a virulent strain of Entamoeba histolytica
    • Edman U., Meza I., and Agabian N. Genomic and cDNA actin sequences from a virulent strain of Entamoeba histolytica. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 3024-3028
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 3024-3028
    • Edman, U.1    Meza, I.2    Agabian, N.3
  • 8
    • 0025090854 scopus 로고
    • Characterization of an immuno-dominant variable surface antigen from pathogenic and nonpathogenic Entamoeba histolytica
    • Edman U., Meraz M.A., Rausser S., Agabian N., and Meza I. Characterization of an immuno-dominant variable surface antigen from pathogenic and nonpathogenic Entamoeba histolytica. J. Exp. Med. 172 (1990) 879-888
    • (1990) J. Exp. Med. , vol.172 , pp. 879-888
    • Edman, U.1    Meraz, M.A.2    Rausser, S.3    Agabian, N.4    Meza, I.5
  • 9
    • 0036571628 scopus 로고    scopus 로고
    • Separable potential polyadenylation and cleavage motifs in Trichomonas vaginalis mRNAs
    • Espinosa N., Hernandez R., Lopez-Griego L., and Lopez-Villasenor I. Separable potential polyadenylation and cleavage motifs in Trichomonas vaginalis mRNAs. Gene 289 (2002) 81-86
    • (2002) Gene , vol.289 , pp. 81-86
    • Espinosa, N.1    Hernandez, R.2    Lopez-Griego, L.3    Lopez-Villasenor, I.4
  • 10
    • 0037089139 scopus 로고    scopus 로고
    • Probabilistic prediction of Saccharomyces cerevisiae mRNA 3′-processing sites
    • Graber J.H., McAllister G.D., and Smith T.F. Probabilistic prediction of Saccharomyces cerevisiae mRNA 3′-processing sites. Nucleic Acids Res. 30 (2002) 1851-1858
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1851-1858
    • Graber, J.H.1    McAllister, G.D.2    Smith, T.F.3
  • 11
    • 0031610367 scopus 로고    scopus 로고
    • U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U1 70K and poly(A) polymerase
    • Gunderson S.I., Polycarpou-Schwarz M., and Mattaj I.W. U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U1 70K and poly(A) polymerase. Mol. Cell 1 (1998) 255-264
    • (1998) Mol. Cell , vol.1 , pp. 255-264
    • Gunderson, S.I.1    Polycarpou-Schwarz, M.2    Mattaj, I.W.3
  • 12
    • 3242672609 scopus 로고    scopus 로고
    • A probabilistic model of 3′ end formation in Caenorhabditis elegans
    • Hajarnavis A., Korf I., and Durbin R. A probabilistic model of 3′ end formation in Caenorhabditis elegans. Nucleic Acids Res. 32 (2004) 3392-3399
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3392-3399
    • Hajarnavis, A.1    Korf, I.2    Durbin, R.3
  • 13
    • 25844497003 scopus 로고    scopus 로고
    • Bioinformatic identification of candidate cis-regulatory elements involved in human mRNA polyadenylation
    • Hu J., Lutz C.S., Wilusz J., and Tian B. Bioinformatic identification of candidate cis-regulatory elements involved in human mRNA polyadenylation. RNA 11 (2005) 1485-1493
    • (2005) RNA , vol.11 , pp. 1485-1493
    • Hu, J.1    Lutz, C.S.2    Wilusz, J.3    Tian, B.4
  • 15
    • 0001974063 scopus 로고    scopus 로고
    • Epidemiology
    • Ravdin J.I. (Ed), Imperial College Press, London
    • Jackson T.F. Epidemiology. In: Ravdin J.I. (Ed). Amebiasis (2000), Imperial College Press, London 47-63
    • (2000) Amebiasis , pp. 47-63
    • Jackson, T.F.1
  • 18
    • 27244444905 scopus 로고    scopus 로고
    • Compilation of mRNA polyadenylation signals in Arabidopsis revealed a new signal element and potential secondary structures
    • Loke J.C., Stahlberg E.A., Strenski D.G., Haas B.J., Wood P.C., and Li Q.Q. Compilation of mRNA polyadenylation signals in Arabidopsis revealed a new signal element and potential secondary structures. Plant Physiol. 138 (2005) 1457-1468
    • (2005) Plant Physiol. , vol.138 , pp. 1457-1468
    • Loke, J.C.1    Stahlberg, E.A.2    Strenski, D.G.3    Haas, B.J.4    Wood, P.C.5    Li, Q.Q.6
  • 19
    • 0037500222 scopus 로고    scopus 로고
    • EhPgp5 mRNA stability is a regulatory event in the Entamoeba histolytica MDR phenotype
    • López-Camarillo C., Luna-Arias J.P., Marchat L.A., and Orozco E. EhPgp5 mRNA stability is a regulatory event in the Entamoeba histolytica MDR phenotype. J. Biol. Chem. 278 (2003) 11273-11280
    • (2003) J. Biol. Chem. , vol.278 , pp. 11273-11280
    • López-Camarillo, C.1    Luna-Arias, J.P.2    Marchat, L.A.3    Orozco, E.4
  • 20
    • 20444442702 scopus 로고    scopus 로고
    • Entamoeba histolytica: comparative genomics of the pre-mRNA 3′ end processing machinery
    • López-Camarillo C., Orozco E., and Marchat L.A. Entamoeba histolytica: comparative genomics of the pre-mRNA 3′ end processing machinery. Exp. Parasitol. 110 (2005) 184-190
    • (2005) Exp. Parasitol. , vol.110 , pp. 184-190
    • López-Camarillo, C.1    Orozco, E.2    Marchat, L.A.3
  • 21
    • 0031840978 scopus 로고    scopus 로고
    • Regulation of alternative polyadenylation by U1 snRNPs and SRp20
    • Lou H., Neugebauer K.M., Gagel R.F., and Berget S.M. Regulation of alternative polyadenylation by U1 snRNPs and SRp20. Mol. Cell. Biol. 18 (1998) 4977-4985
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4977-4985
    • Lou, H.1    Neugebauer, K.M.2    Gagel, R.F.3    Berget, S.M.4
  • 22
    • 23144440350 scopus 로고    scopus 로고
    • DINAMelt web server for nucleic acid melting prediction
    • Markham N.R., and Zuker M. DINAMelt web server for nucleic acid melting prediction. Nucleic Acids Res. 33 (2005) 577-581
    • (2005) Nucleic Acids Res. , vol.33 , pp. 577-581
    • Markham, N.R.1    Zuker, M.2
  • 23
    • 0025577816 scopus 로고
    • Upstream sequences other than AAUAAA are required for efficient messenger RNA 3′-end formation in plants
    • Mogen B.D., MacDonald M.H., Graybosch R., and Hung A.G. Upstream sequences other than AAUAAA are required for efficient messenger RNA 3′-end formation in plants. Plant Cell 2 (1990) 1261-1272
    • (1990) Plant Cell , vol.2 , pp. 1261-1272
    • Mogen, B.D.1    MacDonald, M.H.2    Graybosch, R.3    Hung, A.G.4
  • 24
    • 0032406914 scopus 로고    scopus 로고
    • Cloning and bacterial expression of adenosine-5′-triphosphate sulfurylase from the enteric protozoan parasite Entamoeba histolytica
    • Nozaki T., Arase T., Shigeta Y., Asai T., Leustek T., and Takeuchi T. Cloning and bacterial expression of adenosine-5′-triphosphate sulfurylase from the enteric protozoan parasite Entamoeba histolytica. Biochim. Biophys. Acta 1429 (1998) 284-291
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 284-291
    • Nozaki, T.1    Arase, T.2    Shigeta, Y.3    Asai, T.4    Leustek, T.5    Takeuchi, T.6
  • 25
    • 0024447603 scopus 로고
    • Ultrastructural localization of giardins to the edges of disk microribbons of Giardia lamblia and the nucleotide and deduced protein sequence of alpha giardin
    • Peattie D.A., Alonso R.A., Hein A., and Caulfield J.P. Ultrastructural localization of giardins to the edges of disk microribbons of Giardia lamblia and the nucleotide and deduced protein sequence of alpha giardin. J. Cell. Biol. 109 (1989) 2323-2335
    • (1989) J. Cell. Biol. , vol.109 , pp. 2323-2335
    • Peattie, D.A.1    Alonso, R.A.2    Hein, A.3    Caulfield, J.P.4
  • 26
    • 2342505693 scopus 로고    scopus 로고
    • New perspectives on connecting messenger RNA 3′ end formation to transcription
    • Proudfoot N. New perspectives on connecting messenger RNA 3′ end formation to transcription. Curr. Opin. Cell. Biol. 16 (2004) 272-278
    • (2004) Curr. Opin. Cell. Biol. , vol.16 , pp. 272-278
    • Proudfoot, N.1
  • 27
    • 0030592464 scopus 로고    scopus 로고
    • Developmentally regulated transcripts and evidence of differential mRNA processing in Giardia lamblia
    • Que X., Svard S.G., Meng T.C., Hetsko M.L., Aley S.B., and Gillin F.D. Developmentally regulated transcripts and evidence of differential mRNA processing in Giardia lamblia. Mol. Biochem. Parasitol. 81 (1996) 101-110
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 101-110
    • Que, X.1    Svard, S.G.2    Meng, T.C.3    Hetsko, M.L.4    Aley, S.B.5    Gillin, F.D.6
  • 29
    • 0348048788 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of a serine proteinase inhibitor gene from Entamoeba histolytica
    • Riahi Y., Siman-Tov R., and Ankri S. Molecular cloning, expression and characterization of a serine proteinase inhibitor gene from Entamoeba histolytica. Mol. Biochem. Parasitol. 133 (2004) 153-162
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 153-162
    • Riahi, Y.1    Siman-Tov, R.2    Ankri, S.3
  • 30
    • 0029920734 scopus 로고    scopus 로고
    • Cloning and expression of an Entamoeba histolytica NAPD+(-)dependent alcohol dehydrogenase gene
    • Rodriguez M.A., Baez-Camargo M., Delgadillo D.M., and Orozco E. Cloning and expression of an Entamoeba histolytica NAPD+(-)dependent alcohol dehydrogenase gene. Biochim. Biophys. Acta 1306 (1996) 23-26
    • (1996) Biochim. Biophys. Acta , vol.1306 , pp. 23-26
    • Rodriguez, M.A.1    Baez-Camargo, M.2    Delgadillo, D.M.3    Orozco, E.4
  • 31
    • 0028351948 scopus 로고
    • The contribution of AAUAAA and the upstream element UUUGUA to the efficiency of mRNA 3′-end formation in plants
    • Rothnie H.M., Reid J., and Hohn T. The contribution of AAUAAA and the upstream element UUUGUA to the efficiency of mRNA 3′-end formation in plants. EMBO J. 13 (1994) 2200-2210
    • (1994) EMBO J. , vol.13 , pp. 2200-2210
    • Rothnie, H.M.1    Reid, J.2    Hohn, T.3
  • 32
    • 0344333484 scopus 로고    scopus 로고
    • Cloning and heterologous expression of Entamoeba histolytica adenylate kinase and uridylate/cytidylate kinase
    • Sanchez L.B., and Muller M. Cloning and heterologous expression of Entamoeba histolytica adenylate kinase and uridylate/cytidylate kinase. Gene 209 (1998) 219-228
    • (1998) Gene , vol.209 , pp. 219-228
    • Sanchez, L.B.1    Muller, M.2
  • 33
    • 0028023825 scopus 로고
    • Cloning, genomic organization and transcription of the Entamoeba histolytica alpha-tubulin-encoding gene
    • Sanchez M.A., Peattie D.A., Wirth D., and Orozco E. Cloning, genomic organization and transcription of the Entamoeba histolytica alpha-tubulin-encoding gene. Gene 146 (1994) 239-244
    • (1994) Gene , vol.146 , pp. 239-244
    • Sanchez, M.A.1    Peattie, D.A.2    Wirth, D.3    Orozco, E.4
  • 34
    • 0025951254 scopus 로고
    • Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction
    • Tachibana H., Ihara S., Kobayashi S., Kaneda Y., Takeuchi T., and Watanabe Y. Differences in genomic DNA sequences between pathogenic and nonpathogenic isolates of Entamoeba histolytica identified by polymerase chain reaction. J. Clin. Microbiol. 29 (1991) 2234-2239
    • (1991) J. Clin. Microbiol. , vol.29 , pp. 2234-2239
    • Tachibana, H.1    Ihara, S.2    Kobayashi, S.3    Kaneda, Y.4    Takeuchi, T.5    Watanabe, Y.6
  • 35
    • 0025946099 scopus 로고
    • Pathogenic and nonpathogenic Entamoeba histolytica: identification and molecular cloning of an iron-containing superoxide dismutase
    • Tannich E., Bruchhaus I., Walter R.D., and Horstmann R.D. Pathogenic and nonpathogenic Entamoeba histolytica: identification and molecular cloning of an iron-containing superoxide dismutase. Mol. Biochem. Parasitol. 49 (1991) 61-71
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 61-71
    • Tannich, E.1    Bruchhaus, I.2    Walter, R.D.3    Horstmann, R.D.4
  • 36
    • 0025794045 scopus 로고
    • Homologous cysteine proteinases of pathogenic and nonpathogenic Entamoeba histolytica. Differences in structure and expression
    • Tannich E., Scholze H., Nickel R., and Horstmann R.D. Homologous cysteine proteinases of pathogenic and nonpathogenic Entamoeba histolytica. Differences in structure and expression. J. Biol. Chem. 266 (1991) 4798-4803
    • (1991) J. Biol. Chem. , vol.266 , pp. 4798-4803
    • Tannich, E.1    Scholze, H.2    Nickel, R.3    Horstmann, R.D.4
  • 37
    • 0035145592 scopus 로고    scopus 로고
    • hnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells
    • Veraldi K.L., Arhin G.K., Martincic K., Chung-Ganster L.H., Wilusz J., and Milcarek C. hnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells. Mol. Cell. Biol. 21 (2001) 1228-1238
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1228-1238
    • Veraldi, K.L.1    Arhin, G.K.2    Martincic, K.3    Chung-Ganster, L.H.4    Wilusz, J.5    Milcarek, C.6
  • 38
    • 33646919107 scopus 로고    scopus 로고
    • Stress by heat shock induces massive down regulation of genes and allows differential allelic expression of the Gal/GalNAc lectin in Entamoeba histolytica
    • Weber C., Guigon G., Bouchier C., Frangeul L., Moreira S., Sismeiro O., Gouyette C., Mirelman D., Coppee J.Y., and Guillen N. Stress by heat shock induces massive down regulation of genes and allows differential allelic expression of the Gal/GalNAc lectin in Entamoeba histolytica. Eukaryot. Cell 5 (2006) 871-875
    • (2006) Eukaryot. Cell , vol.5 , pp. 871-875
    • Weber, C.1    Guigon, G.2    Bouchier, C.3    Frangeul, L.4    Moreira, S.5    Sismeiro, O.6    Gouyette, C.7    Mirelman, D.8    Coppee, J.Y.9    Guillen, N.10
  • 39
    • 0025177037 scopus 로고
    • A multicomponent complex is required for the AAUAAA-dependent cross-linking of a 64-kilodalton protein to polyadenylation substrates
    • Wilusz J., Shenk T., Takagaki Y., and Manley J.L. A multicomponent complex is required for the AAUAAA-dependent cross-linking of a 64-kilodalton protein to polyadenylation substrates. Mol. Cell. Biol. 10 (1990) 1244-1248
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1244-1248
    • Wilusz, J.1    Shenk, T.2    Takagaki, Y.3    Manley, J.L.4
  • 40
    • 0026665799 scopus 로고
    • Ubiquitin of Entamoeba histolytica deviates in six amino acid residues from the consensus of all other known ubiquitins
    • Wostmann C., Tannich E., and Bakker-Grunwald T. Ubiquitin of Entamoeba histolytica deviates in six amino acid residues from the consensus of all other known ubiquitins. FEBS Lett. 308 (1992) 54-58
    • (1992) FEBS Lett. , vol.308 , pp. 54-58
    • Wostmann, C.1    Tannich, E.2    Bakker-Grunwald, T.3
  • 41
    • 0033059981 scopus 로고    scopus 로고
    • Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis
    • Zhao J., Hyman L., and Moore C. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol. Mol. Biol. Rev. 63 (1999) 405-445
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 405-445
    • Zhao, J.1    Hyman, L.2    Moore, C.3
  • 42
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acid Res. 31 (2003) 3406-3415
    • (2003) Nucleic Acid Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.