The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

COX1.3  -  endonuclease

Kazachstania servazzii

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of COX1.3


High impact information on COX1.3


Chemical compound and disease context of COX1.3

  • The assay employs dimer-specific, endonuclease activities from Micrococcus luteus together with DNA sedimentation through calibrated, alkaline sucrose gradients to detect endonuclease-induced, single-strand breaks [10].
  • The action of an endonuclease from Micrococcus luteus that operates on UV damage in DNA overlaps with that of DNA photolyase from yeast: homo- and heterocyclobutane dipyrimidines in DNA are substrates for both enzymes, but pyrimidine adducts or the "spore photoproduct" in DNA are not [11].

Biological context of COX1.3

  • One endonuclease, which we call YZ endo, is present only in yeast strains that are undergoing mating-type interconversion [12].
  • For aI2 this predominantly occurs by reverse transcription of unspliced precursor RNA at a break in double-strand DNA made by an endonuclease encoded by the intron [13].
  • One such enzyme is the Saccharomyces cerevisiae Dna2 helicase/endonuclease, which is essential for cell viability and is well suited to removing RNA primers of Okazaki fragments [14].
  • Accuracy in transfer RNA (tRNA) splicing is essential for the formation of functional tRNAs, and hence for gene expression, in both Eukaryotes and Archaea. The specificity for recognition of the tRNA precursor (pre-tRNA) resides in the endonuclease, which removes the intron by making two independent endonucleolytic cleavages [15].
  • The gene, called CCE1 (cruciform cutting endonuclease), was sequenced and found to have an open reading frame encoding a 41 kDa protein [16].

Anatomical context of COX1.3

  • The Saccharomyces cerevisiae HO gene, which encodes a site-specific endonuclease, is transcribed in the parent (mother) cell but not in the daughter (bud) cell [17].
  • An endonuclease with multiple cutting sites, Endo.SceI, initiates genetic recombination at its cutting site in yeast mitochondria [18].
  • To determine whether XpF/Ercc1 endonuclease has a similar role in mitotic recombination, we targeted the APRT locus in Chinese hamster ovary ERCC1(+) and ERCC1(-) cell lines with insertion vectors having long or short terminal non-homologies flanking each side of a double-strand break [19].
  • Since the other tRNA splicing component, the endonuclease, has the characteristics of an integral membrane protein, we hypothesize that it constitutes the site for the interaction of ligase with the nuclear envelope [20].
  • The data are thus consistent with the idea that frequent horizontal transmission is necessary for the long-term persistence of homing endonuclease genes, and further, that this requirement limits these genes to organisms with easily accessible germ lines [21].

Associations of COX1.3 with chemical compounds

  • The mitochondrial DNA segments of two independently isolated rho- clones of S. cerevisiae carrying a genetic marker for a threonine tRNA have been characterized by restriction endonuclease analysis and DNA sequencing [22].
  • The activity of the wheat germ endonuclease is stimulated 3-fold by the non-ionic detergent Triton X-100 [23].
  • tRNA splicing in the yeast Saccharomyces cerevisiae requires an endonuclease to excise the intron, tRNA ligase to join the tRNA half-molecules, and 2'-phosphotransferase to transfer the splice junction 2'-phosphate from ligated tRNA to NAD, producing ADP ribose 1"-2" cyclic phosphate (Appr>p) [24].
  • Moreover, changing the ratios of the MAG 3-methyladenine DNA glycosylase and the APN1 AP endonuclease had profound effects on spontaneous mutation rates [25].
  • DNaseY, a Ca(2+)- and Mg(2+)-dependent endonuclease, has been implicated in apoptotic DNA degradation; however, the molecular mechanisms controlling its involvement in this process have not been fully elucidated [26].

Other interactions of COX1.3

  • We have tested the effects of SUV3-1 on a mutant containing two adjacent transversions within a dodecamer at the 3' end of fit1, a gene located within the 1,143-base-pair intron of the 21S rRNA gene, whose product is a site-specific endonuclease required in crosses for the quantitative transmission of that intron to 21S alleles that lack it [27].
  • The primary transcripts are cleaved by an endonuclease to give tRNAAsp with a mature 5' terminus, and a pre-tRNAArg monomer with a 5' leader and 3' trailer sequences [28].
  • Transcripts from this hybrid gene were found to be processed by endonuclease and ligase at the tRNATrp exon-intron boundaries [29].
  • A second endonuclease cleavage of pre-tRNAArg generates the mature 5' terminus of tRNAArg [28].

Analytical, diagnostic and therapeutic context of COX1.3


  1. Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease. Sijbers, A.M., de Laat, W.L., Ariza, R.R., Biggerstaff, M., Wei, Y.F., Moggs, J.G., Carter, K.C., Shell, B.K., Evans, E., de Jong, M.C., Rademakers, S., de Rooij, J., Jaspers, N.G., Hoeijmakers, J.H., Wood, R.D. Cell (1996) [Pubmed]
  2. The effects of Escherichia coli and yeast DNA insertions on the growth of lambda bacteriophage. Cameron, J.R., Davis, R.W. Science (1977) [Pubmed]
  3. Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: implications for nucleotide excision repair and Cockayne syndrome. Habraken, Y., Sung, P., Prakash, S., Prakash, L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Cleavage of yeast and bacteriophage T7 genomes at a single site using the rare cutter endonuclease I-Sce I. Thierry, A., Perrin, A., Boyer, J., Fairhead, C., Dujon, B., Frey, B., Schmitz, G. Nucleic Acids Res. (1991) [Pubmed]
  5. Three additional genes involved in pyrimidine dimer removal in Saccharomyces cerevisiae: RAD7, RAD14 and MMS19. Prakash, L., Prakash, S. Mol. Gen. Genet. (1979) [Pubmed]
  6. Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation. Paushkin, S.V., Patel, M., Furia, B.S., Peltz, S.W., Trotta, C.R. Cell (2004) [Pubmed]
  7. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Duan, X., Gimble, F.S., Quiocho, F.A. Cell (1997) [Pubmed]
  8. At least 1400 base pairs of 5'-flanking DNA is required for the correct expression of the HO gene in yeast. Nasmyth, K. Cell (1985) [Pubmed]
  9. Genetic recombination of homologous plasmids catalyzed by cell-free extracts of Saccharomyces cerevisiae. Symington, L.S., Fogarty, L.M., Kolodner, R. Cell (1983) [Pubmed]
  10. Removal of pyrimidine dimers from Saccharomyces cerevisiae nuclear DNA under nongrowth conditions as detected by a sensitive, enzymatic assay. Reynolds, R.J. Mutat. Res. (1978) [Pubmed]
  11. Substrate specificity of Micrococcus luteus UV endonuclease and its overlap with DNA photolyase activity. Patrick, M.H. Basic Life Sci. (1975) [Pubmed]
  12. A site-specific endonuclease essential for mating-type switching in Saccharomyces cerevisiae. Kostriken, R., Strathern, J.N., Klar, A.J., Hicks, J.B., Heffron, F. Cell (1983) [Pubmed]
  13. Efficient integration of an intron RNA into double-stranded DNA by reverse splicing. Yang, J., Zimmerly, S., Perlman, P.S., Lambowitz, A.M. Nature (1996) [Pubmed]
  14. RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes. Bae, S.H., Bae, K.H., Kim, J.A., Seo, Y.S. Nature (2001) [Pubmed]
  15. Conservation of substrate recognition mechanisms by tRNA splicing endonucleases. Fabbri, S., Fruscoloni, P., Bufardeci, E., Di Nicola Negri, E., Baldi, M.I., Attardi, D.G., Mattoccia, E., Tocchini-Valentini, G.P. Science (1998) [Pubmed]
  16. Identification and characterization of yeast mutants and the gene for a cruciform cutting endonuclease. Kleff, S., Kemper, B., Sternglanz, R. EMBO J. (1992) [Pubmed]
  17. The mother-daughter mating type switching asymmetry of budding yeast is not conferred by the segregation of parental HO gene DNA strands. Klar, A.J. Genes Dev. (1987) [Pubmed]
  18. An endonuclease with multiple cutting sites, Endo.SceI, initiates genetic recombination at its cutting site in yeast mitochondria. Nakagawa, K., Morishima, N., Shibata, T. EMBO J. (1992) [Pubmed]
  19. Role of ERCC1 in removal of long non-homologous tails during targeted homologous recombination. Adair, G.M., Rolig, R.L., Moore-Faver, D., Zabelshansky, M., Wilson, J.H., Nairn, R.S. EMBO J. (2000) [Pubmed]
  20. The subnuclear localization of tRNA ligase in yeast. Clark, M.W., Abelson, J. J. Cell Biol. (1987) [Pubmed]
  21. Recurrent invasion and extinction of a selfish gene. Goddard, M.R., Burt, A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  22. Assembly of the mitochondrial membrane system: sequences of yeast mitochondrial valine and an unusual threonine tRNA gene. Li, M., Tzagoloff, A. Cell (1979) [Pubmed]
  23. A cell-free plant extract for accurate pre-tRNA processing, splicing and modification. Stange, N., Beier, H. EMBO J. (1987) [Pubmed]
  24. A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli. Spinelli, S.L., Malik, H.S., Consaul, S.A., Phizicky, E.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  25. In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells. Xiao, W., Samson, L. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  26. Regulation of DNaseY activity by actinin-alpha4 during apoptosis. Liu, Q.Y., Lei, J.X., LeBlanc, J., Sodja, C., Ly, D., Charlebois, C., Walker, P.R., Yamada, T., Hirohashi, S., Sikorska, M. Cell Death Differ. (2004) [Pubmed]
  27. Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene. Zhu, H., Conrad-Webb, H., Liao, X.S., Perlman, P.S., Butow, R.A. Mol. Cell. Biol. (1989) [Pubmed]
  28. Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae. Engelke, D.R., Gegenheimer, P., Abelson, J. J. Biol. Chem. (1985) [Pubmed]
  29. Splicing of intron-containing tRNATrp by the archaeon Haloferax volcanii occurs independent of mature tRNA structure. Armbruster, D.W., Daniels, C.J. J. Biol. Chem. (1997) [Pubmed]
  30. Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays. Brenner, S., Johnson, M., Bridgham, J., Golda, G., Lloyd, D.H., Johnson, D., Luo, S., McCurdy, S., Foy, M., Ewan, M., Roth, R., George, D., Eletr, S., Albrecht, G., Vermaas, E., Williams, S.R., Moon, K., Burcham, T., Pallas, M., DuBridge, R.B., Kirchner, J., Fearon, K., Mao, J., Corcoran, K. Nat. Biotechnol. (2000) [Pubmed]
  31. Circular DNA of a yeast episome with two inverted repeats: structural analysis by a restriction enzyme and electron microscopy. Guerineau, M., Grandchamp, C., Slonimski, P.P. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  32. A functional prepro-alpha-factor gene in Saccharomyces yeasts can contain three, four, or five repeats of the mature pheromone sequence. Brake, A.J., Julius, D.J., Thorner, J. Mol. Cell. Biol. (1983) [Pubmed]
  33. Relationships between respiration and susceptibility to azole antifungals in Candida glabrata. Brun, S., Aubry, C., Lima, O., Filmon, R., Bergès, T., Chabasse, D., Bouchara, J.P. Antimicrob. Agents Chemother. (2003) [Pubmed]
  34. Structural and functional analysis of the homing endonuclease PI-sceI by limited proteolytic cleavage and molecular cloning of partial digestion products. Pingoud, V., Grindl, W., Wende, W., Thole, H., Pingoud, A. Biochemistry (1998) [Pubmed]
WikiGenes - Universities