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RBL2  -  Rbl2p

Saccharomyces cerevisiae S288c

Synonyms: CFA, Tubulin-folding cofactor A, Tubulin-specific chaperone A, YOR265W
 
 
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Disease relevance of RBL2

  • Rescue of beta-tubulin toxicity requires a minimal but substoichiometric ratio of Rbl2p to beta-tubulin [1].
  • To explore this hypothesis, E. coli expressing P, type 1, S, colonization factor antigen I (CFA/I), or CFA/II fimbriae was grown in the presence of salicylate, bismuth salts, NaCl, and nonfermented sugars [2].
 

High impact information on RBL2

 

Biological context of RBL2

  • Overexpression of the beta-tubulin binding protein Rbl2p/cofactor A is lethal in yeast cells expressing a mutant alpha-tubulin, tub1-724, that produces unstable heterodimer [6].
  • These include the lethality of tub1-724 haploid cells when the beta-tubulin-binding protein Rbl2p is either overexpressed or absent [4].
 

Associations of RBL2 with chemical compounds

  • Variable protection against malaria blood-stage infection has been demonstrated in mice following parenteral immunization with the highly conserved 19 kD carboxylterminal fragment of the merozoite surface protein-1 (MSP119) using CFA/IFA and other adjuvants [7].
 

Physical interactions of RBL2

  • Residues in the N termini and the loops of the Rbl2 homodimer appear to mediate binding to beta-tubulin [8].
  • Luv1p [corrected] can be isolated in a complex containing Rbl2p [9].
 

Regulatory relationships of RBL2

 

Other interactions of RBL2

  • We have used computational docking and site-directed mutagenesis to generate a model of the Rbl2-Tub2 complex from the solved structures of these two proteins [8].
  • Here we describe the identification of a novel yeast gene, LUV1 [corrected], that interacts genetically with RBL2 [9].

References

  1. Protection from free beta-tubulin by the beta-tubulin binding protein Rbl2p. Abruzzi, K.C., Smith, A., Chen, W., Solomon, F. Mol. Cell. Biol. (2002) [Pubmed]
  2. Effect of salicylate, bismuth, osmolytes, and tetracycline resistance on expression of fimbriae by Escherichia coli. Kunin, C.M., Hua, T.H., Guerrant, R.L., Bakaletz, L.O. Infect. Immun. (1994) [Pubmed]
  3. Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo. Archer, J.E., Vega, L.R., Solomon, F. Cell (1995) [Pubmed]
  4. An alpha-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins. Vega, L.R., Fleming, J., Solomon, F. Mol. Biol. Cell (1998) [Pubmed]
  5. Modulation of tubulin polypeptide ratios by the yeast protein Pac10p. Alvarez, P., Smith, A., Fleming, J., Solomon, F. Genetics (1998) [Pubmed]
  6. Function of tubulin binding proteins in vivo. Fleming, J.A., Vega, L.R., Solomon, F. Genetics (2000) [Pubmed]
  7. Intranasal immunization with yeast-expressed 19 kD carboxyl-terminal fragment of Plasmodium yoelii merozoite surface protein-1 (yMSP119) induces protective immunity to blood stage malaria infection in mice. Hirunpetcharat, C., Stanisic, D., Liu, X.Q., Vadolas, J., Strugnell, R.A., Lee, R., Miller, L.H., Kaslow, D.C., Good, M.F. Parasite Immunol. (1998) [Pubmed]
  8. Model for the yeast cofactor A-beta-tubulin complex based on computational docking and mutagensis. You, L., Gillilan, R., Huffaker, T.C. J. Mol. Biol. (2004) [Pubmed]
  9. Regulation of tubulin polypeptides and microtubule function: Luv1p [correction of Rki1p] interacts with the beta-tubulin binding protein Rbl2p. Smith, A.M., Archer, J.E., Solomon, F. Chromosoma (1998) [Pubmed]
  10. The Arabidopsis TUBULIN-FOLDING COFACTOR A gene is involved in the control of the alpha/beta-tubulin monomer balance. Kirik, V., Grini, P.E., Mathur, J., Klinkhammer, I., Adler, K., Bechtold, N., Herzog, M., Bonneville, J.M., Hülskamp, M. Plant Cell (2002) [Pubmed]
 
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