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RIB2  -  bifunctional DRAP deaminase/tRNA...

Saccharomyces cerevisiae S288c

Synonyms: Bifunctional protein RIB2, PUS8, YOL066C
 
 
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Disease relevance of RIB2

  • Five mutations in two genetically distinct erythromycin resistance loci map in the 23S rDNA of C. reinhardtii, at positions equivalent to E. coli 2057-2058 and 2611, corresponding to the rib3 and rib2 loci of yeast mitochondria respectively [1].
 

High impact information on RIB2

  • By combining genetic and biochemical analyses, we demonstrate that two enzymes, Rib2/Pus8p and Pus9p, are required for Psi32 formation in cytoplasmic and mitochondrial tRNAs, respectively [2].
  • Indeed, Rib2/Pus8p displays two distinct catalytic activities involved in completely unrelated metabolism: its C-terminal domain has a DRAP-deaminase activity required for riboflavin biogenesis in the cytoplasm, whereas its N-terminal domain carries the tRNA:Psi32-synthase activity [2].
  • Erythromycin and spiramycin resistance mutations of yeast mitochondria: nature of the rib2 locus in the large ribosomal RNA gene [3].
  • In addition, we have constructed a physical map with a resolution of about 200 bp of a HapII fragment of 1850 bp long, which carries the loci omega, RIB-1 and probably RIB-2 [4].
  • Recombination studies showed that the two mitochondrial mucidin loci were not allelic with other mitochondrial loci RIB1, RIB2 and OLI1 [5].
 

Biological context of RIB2

  • 4. In all our rho+ as well as rho- strains there is a one-to-one correlation between the omega+ phenotype, the ability to transmit the omega+ allele and the presence of a mtDNA segment of about 1000 bp long, located between sequences specifying RIB-3 and sequences corresponding to the loci RIB-1 and RIB-2 [6].
  • A single nucleotide substitution at the rib2 locus of the yeast mitochondrial gene for 21S rRNA confers resistance to erythromycin and cold-sensitive ribosome assembly [7].
 

Anatomical context of RIB2

 

Associations of RIB2 with chemical compounds

  • The effect of riboflavin and iron on 6-hydroxy-2,4,5-triaminopyrimidine synthesis rate was investigated in the cultures of the yeast Pichia guilliermondii (rib2 mutants) with the blocked second reaction to flavinogenesis [8].

References

  1. Antibiotic resistance mutations in the chloroplast 16S and 23S rRNA genes of Chlamydomonas reinhardtii: correlation of genetic and physical maps of the chloroplast genome. Harris, E.H., Burkhart, B.D., Gillham, N.W., Boynton, J.E. Genetics (1989) [Pubmed]
  2. Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae. Behm-Ansmant, I., Grosjean, H., Massenet, S., Motorin, Y., Branlant, C. J. Biol. Chem. (2004) [Pubmed]
  3. Erythromycin and spiramycin resistance mutations of yeast mitochondria: nature of the rib2 locus in the large ribosomal RNA gene. Sor, F., Fukuhara, H. Nucleic Acids Res. (1984) [Pubmed]
  4. Fine structure of the 21S ribosomal RNA region on yeast mitochondria DNA. I. Construction of the physical map and localization of the cistron for the 21S mitochondrial ribosomal RNA. Heyting, C., Meijlink, F.C., Verbeet, M.P., Sanders, J.P., Bos, J.L., Borst, P. Mol. Gen. Genet. (1979) [Pubmed]
  5. Mucidin resistance in yeast. Isolation, characterization and genetic analysis of nuclear and mitochondrial mucidin-resistant mutants of Saccharomyces cerevisiae. Subík, J., Kovácová, V., Takáscová, G. Eur. J. Biochem. (1977) [Pubmed]
  6. Fine structure of the 21S ribosomal RNA region on yeast mitochondrial DNA. III. Physical location of mitochondrial genetic markers and the molecular nature of omega. Heyting, C., Menke, H.H. Mol. Gen. Genet. (1979) [Pubmed]
  7. A single nucleotide substitution at the rib2 locus of the yeast mitochondrial gene for 21S rRNA confers resistance to erythromycin and cold-sensitive ribosome assembly. Cui, Z., Mason, T.L. Curr. Genet. (1989) [Pubmed]
  8. Regulation of 6-hydroxy-2,4,5-triaminopyrimidine synthesis by riboflavin and iron in riboflavin-deficient mutants of Pichia guilliermondii yeast. Shavlovsku, G.M., Logvinenko, E.M., Schlee, D., Koltun, L.V. Biochim. Biophys. Acta (1976) [Pubmed]
 
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