Ciliate protozoa

C, G or T. This is not sufficient to encode the 20 possible amino acids. In triplets of 3 positions, there are 64 possible combinations. Hence, the system uses triplets, called codons. The code for each protein starts with an ATG (start codon) and ends with a TAA, TAG or a TGA (stop codons). The code is almost universal only mitochondria and ciliated protozoa have a different genetic code. 

Ellis JE, Lindmark DC, Williams AG, Lloyd D (1994) Polypeptides of hydrogenosome-enriched fractions from rumen ciliate protozoa and trichomonads immunological studies. FEMS Microbiol Lett 117 211-216... 

Clarke KJ, Finlay BJ, Esteban G, Guhl BE, Embley TM (1993) Cyclidium porcatum N. sp. -a free-living anaerobic scuticociliate containing a stable complex of hydrogenosomes, eubacteria and archaeobacteria. Eur J Protistol 29 262-270 Corliss JO (1979) The ciliated protozoa Characterization, classification, and guide to the literature. Pergamon Press, London... 

Since the first isolation of 2-aminoethanephosphonic acid (171) from rumen ciliate protozoa,95 related compounds (for example, phosphino-lipid96-97 1 72) in considerable number have been found in Nature, and... 

Gall, J. G., ed. (1986) The Molecular Biology of Ciliated Protozoa, Academic Press, Orlando, Florida... 

Many other phospholipids are present in small amounts or in a limited number of species. These include phosphonolipids, which contain a C-P bond and are abundant in ciliate protozoa such as Tetrahymena and in some other invertebrates.26 Phosphonoethyl-amine replaces phosphoethanolamine in these lipids. A consequence of this structural alteration is a high... 

Insulin or insulin-like material is also produced in ciliated protozoa, vertebrate and invertebrate animals, fungi, green plants,349 350 and even in E. coli.351... 

Gilron, G.L. and Lynn, D.H. (1998) Ciliated protozoa as test organisms in toxicity assessments, in P.G. Wells, K. Lee and C. Blaise (eds.), Microscale Testing in Aquatic Toxicology Advances, Techniques, and Practice, CRC Press, Boca Raton, FL, pp. 323-336. 

Kuhlmann, H.W., Kusch, J., and Heckmann, K., Predator-Induced Defenses in Ciliated Protozoa, Tollrian, R. and Harvell, C.D., Eds., Princeton University Press, Princeton, NJ, 1999, chap. 8, 142. 

The code appears to be universal to the extent that synthetic polyribonucleotides seem to code in the same way in mammals, bacteria, and other species, and components of the protein-synthesizing system of various species can operate with components from certain others. Mitochondria and ciliated protozoa have genetic codes slightly different from the standard. For example, in human mitochondria, UGA codes for tryptophan instead of as a termination signal, AUA codes for methionine rather than isoleucine, and AGA and AGG are termination signals rather than coding for arginine. 

Fenchel, T., 1969. The ecology of marine microbenthos. IV. Structure and function of the benthic ecosystem, its chemical and physical factors and the microfauna communities with special reference to the ciliated protozoa. Ophelia, 6 1—182. 

APHA. 1992. Part 8310, Ciliated protozoa. In Standard Methods for the Determination of Water and Wastes, 18th ed. American Public Health Association, American Water Works Association, and the Water Environment Federation, Washington, D.C., pp. 8-45 to 8-47. 

Class I introns were originally discovered in ciliated protozoa and subsequently were found in fungi, bacteriophages, and other organisms. The RNA itself in a class I in-tron has catalytic activity and class I introns remove themselves from primary RNA transcripts by a self-splicing reaction. Class I introns are not true enzymes in that they function only once. The nucleotides in the intron that is spliced out are recycled in the cell. 

The dihydrofolate reductases of animals and of certain eubacteria are monomeric proteins with molecular weights around 20 kDa. Other eubacteria, ciliate, protozoa, plants, and certain viruses specify bifunctional proteins (DHFR-TS) characterized by dihydrofolate reductase and thymidylate synthetase domains. 

Onodera, R., Yamaguchi, Y. and Morimoto, S. (1983) Metabolism of arginine, citrulline, ornithine and proline by starved rumen ciliate protozoa. Agric. Biol. Chem. 47 821-828. 

Arregui L, Muhoz-Fontela C, 5errano 5 et al. Direct visualizadon of the micro tubular cytoskeleton of ciliated protozoa with a fluorescent taxiod. J Eukaryot Microbiol 2002 49 312-318. 

Quinoxaline is a by-product of cooking some food and can inhibit the growth of some ciliate protozoa and plan-pathogenic fungi. The metabolism of this ring system by Pseudomonas putida can provide the quinoxaline cis-5,6-dihydrodiol, 5-hydroxyquinoxaline, and 2(l//)-quinoxalinone. When quinoxaline is metabolized by Streptomyces badius, two different products were isolated. Both of these two products, 2(l//)-quinoxalinone and 3,4-dihydro-2(l/ )-quinoxalinone, were only isolated from the treatment of Streptomyces badius with quinoxaline. Six other Streptomyces species were tested and only produced 2(l//)-quinoxalinone. The mechanism for the formation of 3,4-dihydro-2(l//)-[Pg.548]

Local versus global diversity of microorganisms cryptic diversity of ciliated protozoa. Oikos SO, 220-225. 

Blatterer, H., Foissner, W. (1992). Morphology and infraciliature of some cyrtophorid ciliates (Protozoa, Ciliophora) from freshwater and soil. Archiv fiir Protistenkunde 142, 101-118. 

Foissner, W. (2004b). Two new flagship ciliates (Protozoa. Cillophora) from Venezuela Sleighophrys pustulata and Luporinophrys micelae. European Journal of Protistology 41,99-117. 

Simon, E.M. (1998). Comparison of sequence differences in a variable 23S rRNA domain among sets of cryptic species of ciliated protozoa. Journal of Eukaryotic Microbiology45,91-100. 

Foissner, W., Agatha, S., Berger, H. (2002). Soil ciliates (Protozoa,Ciliophora) from Namibia (Southwest Africa), with emphasis on two contrasting environments, the Etosha Region and the Namib Desert. Denisia 5,1-1459. 

In some ciliated protozoa, the micronucleus and macronucleus have completely separated S phases within the same interphase. The micronucleus usually replicates during a very short interval beginning in late telophase, and the macronucleus does not begin DNA synthesis until after the micronucleus has completed synthesis (McDonald, 1962 Prescott et al., 1962). This asynchrony may be related to the fact that the DNA in the micronucleus is highly condensed and resembles heterochromatin (see p. 9). 

Jenkins, R. A. 1967. Fine structure of division in ciliate protozoa. I. Micronuclear mitosis in Blepharisma. J. Cell. Biol., 34 463-481. 

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