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Gene Review

CBS1  -  Cbs1p

Saccharomyces cerevisiae S288c

Synonyms: COB-specific translational activator protein CBS1, Cytochrome b translational activator protein CBS1, mitochondrial, YDL069C
 
 
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High impact information on CBS1

 

Biological context of CBS1

  • The results exclude the possibility that suppressor genes have been cloned and confirm the conclusion that both genes, CBS1 and CBS2, specifically are involved in translation of mitochondrial COB RNA [4].
  • Here we report on the identification of two unique chromosomal DNA-sequences of 2 kb and 2.3 kb from yeast wild type gene banks which functionally complement cbs1 and cbs2 mutants, respectively [4].
  • CoxIII translation from an mRNA bearing the 5' leader of the mitochondrial gene aap1 was not dependent on CBS1 activity [5].
  • In this paper we show that the CBS1 gene is located on chromosome IV immediately adjacent to COX9, the gene coding for cytochrome c oxidase subunit VIIa [6].
  • Yeast transformants harboring the CBS1 gene under the control of the strong ADC1 promoter on a high copy number plasmid express the mitochondrial CBS1 protein at artificially high levels [7].
 

Anatomical context of CBS1

  • We conclude that the product of the nuclear gene CBS1, or something under its control, acts in the mitochondrion on the cob mRNA 5' leader to activate translation of down-stream coding sequences [5].
  • Based on its solubilization properties the CBS1 protein is presumed to be a component of the mitochondrial membrane; the detergent concentrations needed to release CBS1 from mitochondria are almost the same as for cytochrome c1 [8].
  • CoxIII was translated from a chimeric mRNA bearing the cob leader only when the zygotes contained a wild-type CBS1 gene [5].
  • In accordance with this result is the observation that the steady-state level of CBS1 mRNA of anaerobically grown cells is ninefold lower than that of aerobically cultured cells [6].
  • We demonstrate here by means of blue native gel electrophoresis, density gradient centrifugation and tandem affinity purification that a portion of Cbs1p is also associated with mitochondrial ribosomes [2].
 

Associations of CBS1 with chemical compounds

  • By monitoring the beta-galactosidase activity of a CBS1/lacZ fusion construct we show that expression of CBS1 is subjected to regulation by oxygen and by glucose: the beta-galactosidase activity is elevated threefold in glycerol or galactose grown cells compared to that in glucose grown cells [6].
  • Similarly, a particular M.grisea CBS1 (encoding cystathionine beta-synthase) TAGKO cDNA failed to complement cysteine auxotrophy in a yeast CBS mutant [9].
  • In addition, we demonstrate that the amount of ribosome-associated Cbs1p is elevated in the presence of chloramphenicol, which is known to stall ribosomes on mRNAs [2].
 

Regulatory relationships of CBS1

  • Translation of mitochondrial cytochrome b mRNA in yeast is activated by the product of the nuclear gene CBS1 [10].
 

Other interactions of CBS1

  • In this article I review available data on CBS1p and CBS2p from the initial detection of the genes up to the current investigations on interacting components and the proteins' topology [11].
  • Chromosomal localization and expression of CBS1, a translational activator of cytochrome b in yeast [6].
  • AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency [12].
  • Molecular characterization of a cystathionine beta-synthase gene, CBS1, in Magnaporthe grisea [13].
 

Analytical, diagnostic and therapeutic context of CBS1

References

  1. Intrasteric control of AMPK via the gamma1 subunit AMP allosteric regulatory site. Adams, J., Chen, Z.P., Van Denderen, B.J., Morton, C.J., Parker, M.W., Witters, L.A., Stapleton, D., Kemp, B.E. Protein Sci. (2004) [Pubmed]
  2. Saccharomyces cerevisiae translational activator Cbs1p is associated with translationally active mitochondrial ribosomes. Krause-Buchholz, U., Schöbel, K., Lauffer, S., Rödel, G. Biol. Chem. (2005) [Pubmed]
  3. Identification of functionally important regions of the Saccharomyces cerevisiae mitochondrial translational activator Cbs1p. Krause-Buchholz, U., Tzschoppe, K., Paret, C., Ostermann, K., Rödel, G. Yeast (2000) [Pubmed]
  4. Molecular cloning of the yeast nuclear genes CBS1 and CBS2. Rödel, G., Michaelis, U., Forsbach, V., Kreike, J., Kaudewitz, F. Curr. Genet. (1986) [Pubmed]
  5. The yeast nuclear gene CBS1 is required for translation of mitochondrial mRNAs bearing the cob 5' untranslated leader. Rödel, G., Fox, T.D. Mol. Gen. Genet. (1987) [Pubmed]
  6. Chromosomal localization and expression of CBS1, a translational activator of cytochrome b in yeast. Forsbach, V., Pillar, T., Gottenöf, T., Rödel, G. Mol. Gen. Genet. (1989) [Pubmed]
  7. Over-expression, purification and determination of the proteolytic processing site of the yeast mitochondrial CBS1 protein. Körte, A., Michaelis, U., Lottspeich, F., Rödel, G. Curr. Genet. (1991) [Pubmed]
  8. Association of cytochrome b translational activator proteins with the mitochondrial membrane: implications for cytochrome b expression in yeast. Michaelis, U., Körte, A., Rödel, G. Mol. Gen. Genet. (1991) [Pubmed]
  9. The bacterial transposon Tn7 causes premature polyadenylation of mRNA in eukaryotic organisms: TAGKO mutagenesis in filamentous fungi. Lo, C., Adachi, K., Shuster, J.R., Hamer, J.E., Hamer, L. Nucleic Acids Res. (2003) [Pubmed]
  10. In vitro and in vivo studies on the mitochondrial import of CBS1, a translational activator of cytochrome b in yeast. Körte, A., Forsbach, V., Gottenöf, T., Rödel, G. Mol. Gen. Genet. (1989) [Pubmed]
  11. Translational activator proteins required for cytochrome b synthesis in Saccharomyces cerevisiae. Rödel, G. Curr. Genet. (1997) [Pubmed]
  12. AUG codons in the RNA leader sequences of the yeast PET genes CBS1 and SCO1 have no influence on translation efficiency. Krummeck, G., Gottenöf, T., Rödel, G. Curr. Genet. (1991) [Pubmed]
  13. Molecular characterization of a cystathionine beta-synthase gene, CBS1, in Magnaporthe grisea. Lo, S.C., Hamer, L., Hamer, J.E. Eukaryotic Cell (2002) [Pubmed]
 
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