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Disease relevance of Crithidia


High impact information on Crithidia

  • Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of Crithidia fasciculata [6].
  • To determine the structural features responsible for the curvature of kinetoplast DNA, we studied 13 adenine tracts in Crithidia fasciculata kinetoplast DNA [7].
  • In the presence of functional RT (from human L1, yeast Tyl or Crithidia CRE1), and in the absence of homologous recombination, an HO endonuclease-induced DSB at the mating type (MAT) locus is the primary site at which a marked cDNA is observed among surviving cells [8].
  • Although the COIII gene encoding cytochrome c oxidase subunit III in Trypanosoma brucei is edited along its entire length, the presumably homologous genes in two related trypanosomes, Leishmania tarentolae and Crithidia fasciculata, are only modestly edited at their 5' ends [9].
  • The cofactor was purified from the insect trypanosomatid Crithidia fasciculata and identified as a novel glutathione-spermidine conjugate, N1,N8-bis(L-gamma-glutamyl-L-hemicystinyl-glycyl)spermidine, for which the trivial name trypanothione is proposed [10].

Biological context of Crithidia


Anatomical context of Crithidia

  • A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata [16].
  • Crithidia fasciculata cells incubated with [14C]glucose or membranes derived from the same protozoan incubated with GDP-[14C]mannose were found to synthesize a lipid monophosphate mannose [17].
  • We discovered that topoisomerase II catalytic activity in 1.0 M NaCl nuclear extracts from the HL-60/MX2 variant, as measured by the decatenation of Crithidia fasciculata kinetoplast DNA, was reduced 4- to 5-fold compared to that in the parental HL-60 cells [18].
  • Pyruvate kinases of Crithidia luciliae and of Leishmania major, two trypanosomatids which are like T. brucei in containing glycosomes, were also stimulated by fructose 2,6-bisphosphate and inhibited by phosphate [19].
  • Crithidia fasciculata ribosomes were found to be 80S and to dissociate into 58 and 41S subunits; on 5 to 50% sucrose gradients, rRNA was separated into 25, 18, and 5S components [20].

Associations of Crithidia with chemical compounds

  • To identify proteins associated with the condensed form of kDNA in the cell, proteins were reversibly crosslinked to kDNA in whole cells of Crithidia fasciculata by formaldehyde treatment [21].
  • Cells of the insect parasite Crithidia fasciculata incubated with [14C]glucose were found to possess only one lipid-bound oligosaccharide with solubility in chloroform/methanol/water mixtures and net charge similar to the charges of dolichol pyrophosphate derivatives [22].
  • A Crithidia fasciculata single-stranded DNA-binding protein interacts specifically with the guanine-rich heavy strand of this origin-associated sequence (Y. Tzfati, H. Abeliovich, I. Kapeller, and J. Shlomai, Proc. Natl. Acad. Sci. USA 89:6891-6895, 1992) [23].
  • In Crithidia luciliae, this 3'-nucleotidase/nuclease previously has been shown to be highly regulated as purine and/or Pi starvation of this trypanosomatid leads to as much as a 1000-fold increase in enzyme activity [24].
  • Incubation of Crithidia fasciculata cells with [U-14C] glucose led to the synthesis of Man-P-dolichol but not of Glc-P-dolichol [25].

Gene context of Crithidia


Analytical, diagnostic and therapeutic context of Crithidia


  1. A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs. Cerritelli, S.M., Fedoroff, O.Y., Reid, B.R., Crouch, R.J. Nucleic Acids Res. (1998) [Pubmed]
  2. Molecular analyses of anti-DNA antibodies induced by polyomavirus BK in BALB/c mice. Rekvig, O.P., Fredriksen, K., Hokland, K., Moens, U., Traavik, T., Krishnan, M.R., Marion, T. Scand. J. Immunol. (1995) [Pubmed]
  3. Toxicity of 4-nitroquinoline 1-oxide for Crithidia fasciculata. Leon, W., Cruz, F.S., Vasconcellos, M.E. J. Protozool. (1975) [Pubmed]
  4. Biopterin content of human neuroblastoma cells in culture. Albrecht, A.M., Biedler, J.L., Baker, H., Frank, O., Hutner, S.H. Res. Commun. Chem. Pathol. Pharmacol. (1978) [Pubmed]
  5. Determination of anti-ds-DNA antibodies by three different methods: comparison of sensitivity, specificity and correlation with lupus activity index (LAI). Tzioufas, A.G., Terzoglou, C., Stavropoulos, E.D., Athanasiadou, S., Moutsopoulos, H.M. Clin. Rheumatol. (1990) [Pubmed]
  6. Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of Crithidia fasciculata. Melendy, T., Sheline, C., Ray, D.S. Cell (1988) [Pubmed]
  7. The unusual conformation adopted by the adenine tracts in kinetoplast DNA. Burkhoff, A.M., Tullius, T.D. Cell (1987) [Pubmed]
  8. Retrotransposon reverse-transcriptase-mediated repair of chromosomal breaks. Teng, S.C., Kim, B., Gabriel, A. Nature (1996) [Pubmed]
  9. RNA editing as a source of genetic variation. Landweber, L.F., Gilbert, W. Nature (1993) [Pubmed]
  10. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T., Cerami, A. Science (1985) [Pubmed]
  11. Complement interaction with trypanosomatid promastigotes in normal human serum. Domínguez, M., Moreno, I., López-Trascasa, M., Toraño, A. J. Exp. Med. (2002) [Pubmed]
  12. Transcripts from the frameshifted MURF3 gene from Crithidia fasciculata are edited by U insertion at multiple sites. van der Spek, H., van den Burg, J., Croiset, A., van den Broek, M., Sloof, P., Benne, R. EMBO J. (1988) [Pubmed]
  13. A single-stranded DNA-binding protein from Crithidia fasciculata recognizes the nucleotide sequence at the origin of replication of kinetoplast DNA minicircles. Tzfati, Y., Abeliovich, H., Kapeller, I., Shlomai, J. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  14. Characterization of the Crithidia fasciculata mRNA cycling sequence binding proteins. Mahmood, R., Mittra, B., Hines, J.C., Ray, D.S. Mol. Cell. Biol. (2001) [Pubmed]
  15. Aerobic fermentation of glucose by trypanosomatids. Cazzulo, J.J. FASEB J. (1992) [Pubmed]
  16. A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata. Torri, A.F., Englund, P.T. J. Biol. Chem. (1995) [Pubmed]
  17. Novel mannose carrier in the trypanosomatid Crithidia fasciculata behaving as a short alpha-saturated polyprenyl phosphate. Quesada-Allue, L.A., Parodi, A.J. Biochem. J. (1983) [Pubmed]
  18. Mitoxantrone resistance in HL-60 leukemia cells: reduced nuclear topoisomerase II catalytic activity and drug-induced DNA cleavage in association with reduced expression of the topoisomerase II beta isoform. Harker, W.G., Slade, D.L., Drake, F.H., Parr, R.L. Biochemistry (1991) [Pubmed]
  19. Stimulation of Trypanosoma brucei pyruvate kinase by fructose 2,6-bisphosphate. van Schaftingen, E., Opperdoes, F.R., Hers, H.G. Eur. J. Biochem. (1985) [Pubmed]
  20. The ribonucleic acids of Crithidia fasciculata. Morales, N.M., Roberts, J.F. J. Protozool. (1978) [Pubmed]
  21. Isolation of proteins associated with kinetoplast DNA networks in vivo. Xu, C., Ray, D.S. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  22. Pathway of protein glycosylation in the trypanosomatid Crithidia fasciculata. Parodi, A.J., Quesada Allue, L.A., Cazzulo, J.J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  23. A trypanosomal CCHC-type zinc finger protein which binds the conserved universal sequence of kinetoplast DNA minicircles: isolation and analysis of the complete cDNA from Crithidia fasciculata. Abeliovich, H., Tzfati, Y., Shlomai, J. Mol. Cell. Biol. (1993) [Pubmed]
  24. An inducible 3'-nucleotidase/nuclease from the trypanosomatid Crithidia luciliae. Purification and characterization. Neubert, T.A., Gottlieb, M. J. Biol. Chem. (1990) [Pubmed]
  25. N-linked high mannose-type oligosaccharides in the protozoa Crithidia fasciculata and Crithidia harmosa contain galactofuranose residues. Mendelzon, D.H., Parodi, A.J. J. Biol. Chem. (1986) [Pubmed]
  26. Demonstration of autoimmunity in the tight skin-2 mouse: a model for scleroderma. Gentiletti, J., McCloskey, L.J., Artlett, C.M., Peters, J., Jimenez, S.A., Christner, P.J. J. Immunol. (2005) [Pubmed]
  27. 83-kilodalton heat shock proteins of trypanosomes are potent peptide-stimulated ATPases. Nadeau, K., Sullivan, M.A., Bradley, M., Engman, D.M., Walsh, C.T. Protein Sci. (1992) [Pubmed]
  28. Saccharomyces cerevisiae URH1 (encoding uridine-cytidine N-ribohydrolase): functional complementation by a nucleoside hydrolase from a protozoan parasite and by a mammalian uridine phosphorylase. Mitterbauer, R., Karl, T., Adam, G. Appl. Environ. Microbiol. (2002) [Pubmed]
  29. Autoantibody formation in patients with rheumatoid arthritis treated with anti-TNF alpha. Eriksson, C., Engstrand, S., Sundqvist, K.G., Rantapää-Dahlqvist, S. Ann. Rheum. Dis. (2005) [Pubmed]
  30. Structure, genomic organization and transcription of the bifunctional dihydrofolate reductase-thymidylate synthase gene from Crithidia fasciculata. Hughes, D.E., Shonekan, O.A., Simpson, L. Mol. Biochem. Parasitol. (1989) [Pubmed]
  31. Presence of antibodies against a cell-surface protein, cross-reactive with DNA, in systemic lupus erythematosus: a marker of the disease. Jacob, L., Lety, M.A., Choquette, D., Viard, J.P., Jacob, F., Louvard, D., Bach, J.F. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  32. The binding of antihistone antibodies to Crithidia luciliae kinetoplasts is growth cycle-dependent. Deng, J.S., Sontheimer, R.D., Lipscomb, M.F., Gilliam, J.N. Arthritis Rheum. (1985) [Pubmed]
  33. Measurement of increases in anti-double-stranded DNA antibody levels as a predictor of disease exacerbation in systemic lupus erythematosus. A long-term, prospective study. ter Borg, E.J., Horst, G., Hummel, E.J., Limburg, P.C., Kallenberg, C.G. Arthritis Rheum. (1990) [Pubmed]
  34. Enzyme immunoassay for antibodies to native DNA. Specificity and quality of antibodies. Eaton, R.B., Schnneider, G., Schur, P.H. Arthritis Rheum. (1983) [Pubmed]
  35. Isolation of tubulin polyglutamylase from Crithidia; binding to microtubules and tubulin, and glutamylation of mammalian brain alpha- and beta-tubulins. Westermann, S., Schneider, A., Horn, E.K., Weber, K. J. Cell. Sci. (1999) [Pubmed]
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