Cytosolic chaperonin is up-regulated during cell growth. Preferential expression and binding to tubulin at G(1)/S transition through early S phase

J Biol Chem. 1999 Dec 24;274(52):37070-8. doi: 10.1074/jbc.274.52.37070.


The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular chaperone assisting in the folding of actin, tubulin, and other cytosolic proteins. The expression levels of CCT subunits varied among seven mouse cell lines tested but showed a close correlation with growth rate. Both the CCT protein and mRNA levels in the human promyelolytic cell HL60 decreased concomitant with growth arrest during differentiation. More rapid decrease in CCT level occurred when the mouse interleukin (IL)-3-dependent myeloid DA3 cells were starved for IL-3. Readdition of IL-3 caused rapid resumption of CCT synthesis during synchronous growth: the maximum CCT protein and mRNA levels were observed at G(1)/S transition through early S phase. The turnover rate of CCT was nearly constant regardless of growth. Gel filtration and immunoprecipitation analyses indicated that CCT in vivo is associated with tubulin at early S phase, but not at G(0)/G(1) phase. These results demonstrated that CCT expression is strongly up-regulated during cell growth especially from G(1)/S transition to early S phase and is primarily controlled at the mRNA level. CCT appears to play important roles for cell growth by assisting in the folding of tubulin and other proteins.

MeSH terms

  • Animals
  • Cell Division
  • Cell Line
  • Chaperonin Containing TCP-1
  • Chaperonins
  • Cytosol / metabolism*
  • G1 Phase*
  • Heat-Shock Proteins / physiology*
  • Humans
  • Mice
  • Molecular Chaperones / physiology*
  • Protein Folding
  • S Phase*
  • Tubulin / chemistry
  • Tubulin / metabolism*
  • Up-Regulation


  • Heat-Shock Proteins
  • Molecular Chaperones
  • Tcp1 protein, mouse
  • Tubulin
  • Chaperonin Containing TCP-1
  • Chaperonins