Crithidia fasciculata

The D-arabino-D-galactan of cells of the insect protozoon Crithidia fasciculata contains /3-D-(l—>3)-linked D-galactopyranosyl main-chain units, some of which are unsubstituted others are substituted at 0-2 by (single-unit) D-arabinopyranosyl groups. The 13C-n.m.r. spectrum shows that these are only partial structures, as the C-l region contained 8 signals.125... 

Figure 5-16 (A) Electron micrograph of the network of catenated DNA circles in the mitochondrion of the trypanosome Crithidia fasciculata. (B) and (C) The same network after treatment with a topoisomerase from bacteriophage T4 that catalyzes a decatenation to form individual covalently closed circles (Chapter 27). Five times as much enzyme was added in (C) as in (B). Two sizes of circles are present. Most are "minicircles", each containing about 2300 bp but a smaller number of larger 35-kb "maxicircles" are also present. One of these is marked by the arrow. From Marini, Miller, and Englund.183...

Nucleoside hydrolase has been proposed to participate in purine salvage in the trypanosome Crithidia fasciculata. The enzyme hydrolyses the N-glycosidic linkage of the naturally occurring purine and pyrimidine nucleosides. A geometric model of the transition state for nucleoside hydrolase for the reaction (Horenstein et al., 1991)... 

Biopterin (1) is one of the potent natural pteridines isolated from human urine as the growth factor of Crithidia fasciculata It has attracted much attention as a precursor of (67 )-tetrahydrobiopterin, which was known as a coenzyme of aromatic amino acid monooxygenase. ... 

Corynanthe mayumbensis (tetrahydroalstonine), 389 Crithidia fasciculata (biopterin), 375 Crotalaria agatiflora (crotanecine), 240 Crotalaria amagyroids (anacrotine), 244 Crotalaria incana shrub (anacrotine and intergerrimine), 244... 

Large hydron KIEs have been observed in enzymatic reactions at sites far removed from where chemistry is occurring. In enzymatic hydrolysis and transfer reactions of A-ribosides, it has become a common pattern to observe an inverse 4 - H KIE and a normal 5 - H KIE. These KIEs are not intrinsic to the reaction as the KIEs at these positions are negligible in the non-enzymatic reactions. Examples of such enzymatic KIEs include inosine hydrolysis by lU-NH from Crithidia fasciculata, where 4 - H KIE = 0.992, 5 - H KIE = 1.051 and NAD+ hydrolysis by diphtheria toxin A-chain (DTA), where 4 - H KIE = 0.990, 5 - H KIE = 1.032. ... 

Swinkels, B. W., Evers, R. and Borst, P. (1988) The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase of Crithidia fasciculata resides in a carboxy-terminal extension. EMBO J. 7 1159 1165. 

Kidder, G. W., Dewey, V. C. and Nolan, L. L. (1977) Adenine deaminase of a eukaryotic animal cell, Crithidia fasciculata. Arch. Biochem. Biophys. 183 7-12. 

Kidder, G. W. (1984) Characteristics of cytidine aminohydrolase activity in Trypanosoma cruzi and Crithidia fasciculata. J. Protozool. 31 298-300. 

In addition to elevated AdoMet levels, trypanosomes treated with DFMO in vivo experience a six-fold increase in the activity of protein methylase II but not I or III (55). Protein methylase II specifically methylates carboxyl groups of aspartate and glutamate residues. In mammalian cells, histone methylation may be involved in the condensation of euchromatin to heterochromatin prior to mitosis (56-58), and may therefore have a role in gene expression. Aspartate- and glutamate-rich histones have also been characterized from both T. b. brucei and Crithidia fasciculata making these likely substrates for protein methylase II activity (59,60). 

Duschak, V. G. and Cazzulo, J. J. (1990) The histomes of the insect trypanosomatid, Crithidia fasciculata. Biochim. Biophys. Acta. 1040 159-166. 

The cloned trypanothione reductase genes from T. congolense (60) and T. cruzi (61) have been expressed in E. coli, and the enzymes overproduced and purified. The trypanothione reductase genes from Crithidia fasciculata (62,63) and T. brucei (63) have also been cloned and sequenced. Site-directed mutagenesis of either the E. coli glutathione reductase (64) or the T. congolense trypanothione reductase expressed in E. coli (60) has been used to evaluate the role of different residues in the mutually exclusive specificities of trypanothione reductase and glutathione reductase. 

Kusel, J. P., Boveris, A. and Storey, B. T. (1973) H2O2 production and cytochrome c peroxidase activity in mitochondria isolated from the trypanosomatid hemoflagellate Crithidia fasciculata. Arch. Biochem. Biophys. 158 799-804. 

Henderson, G., Fairlamb, A. H. and Cerami, A. (1987) Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei. Mol. Biochem. Parasitol. 24 39-45. 

Shames, S. L., Fairlamb, A. H., Cerami, A. and Walsh, C. T. (1986) Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry 25 3519-3526. 

Aboagye-Kwarteng, T., Smith, K. and Fairlamb, A. H. (1992) Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism. Mol. Microbiol. 6 3089-3099. 

Le Trang, N., Meshnick, S. R., Kitchener, K., Eaton, J. W. and Cerami, A. (1983) Iron-containing superoxide dismutase from Crithidia fasciculata. Purification, characterization, and similarity to leishmanial and trypanosomal enzymes. J. Biol. Chem. 258 125-130. 

Tittawella I. Identification of DNA-binding proteins in the parasitic protozoan Crithidia fasciculata and evidence for their association with the mitochondrial genome. Exp Cell Res 1993 206(1) 143-51. 

Xu CW, Hines JC, Ei l ML et al. Nucleus-encoded histone Hl-like proteins are associated with kinetoplast DNA in the trypanosomatid Crithidia fasciculata. Mol Cell Biol 1996 16(2) 564-76. 

Lukes J, Hines JC, Evans CJ et al. Disruption of the Crithidia fasciculata KAPl gene results in structural rearrangement of the kinetoplast disc. Mol Biochem Parasitol 2001 117(2) 179-86. 

Fei uson ML, Totri AF, Perez-Morga D et aL Kinetoplast DNA replication Mechanistic differences between Trypanosoma brucei and Crithidia fasciculata. J Cell Biol 1994 126(3) 631-9. 

Sugisaki H, Ray DS. DNA sequence of Crithidia fasciculata kinetoplast minidrcles. Mol Biochem Parasitol 1987 23(3) 253-63. 

Birkenmeyer L, Ray DS. Replication of kinetoplast DNA in isolated kinetoplasts from Crithidia fasciculata. Identifrcation of minicircle DNA replication intermediates. J Biol Chem 1986 261(5) 2362-8. 

Birkenmeyer L, Sugjsaki H, Ray DS. Structural characterization of site-specific discontinuities associated with replication origins of minicircle DNA from Crithidia fasciculata. J Biol Chem 1987 262(5) 2384-92. 

Sheline C, Melendy T, Ray DS. Replication of DNA minicircles in kinetoplasts isolated from Crithidia fasciculata Structure of nascent minicircles. Mol Cell Biol 1989 9(l) 169-76. 

Cosgrove WB, Skeen MJ. The cell cycle in Crithidia fasciculata. Temporal tdaiiondiips between synthesis of deoxyribonucleic acid in the nucleus and in the kinetoplast. J Protozool 1970 17(2) 172-7. 

Englund PT. The replication of kinetoplast DNA network in Crithidia fasciculata. Cell 1978 14 157-168. 

Englund PT. Free minicircles of kinetoplast DNA in Crithidia fasciculata. J Biol Chem 1979 254 4895-900. 

Li C, Englund PT. A mitochondrial DNA primase from the trypanosomatid Crithidia fasciculata. J Biol Chem 1997 272(33) 20787-92. 

Torri AF, Englund PT. Purification of a mitochondrial DNA polymerase from Crithidia fasciculata. J Biol Chem 1992 267(7) 4786-92. 

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