- Cdh1 Mutants
- cdh1∆
- sic1∆ cdh1∆
- sic1∆ cdh1∆ GALL-CDC20
- sic1∆ cdc6∆2-49 cdh1∆
- sic1∆ cdc6∆2-49 cdh1∆ GALL-CDC20
- cdh1∆ cdc6∆2-49
- swi5∆ cdh1∆
- swi5∆ cdh1∆ GAL-SIC1
- cln1∆ cln2∆ cdh1∆
- GAL-CLN2 cln1∆ cln2∆ cdh1∆
- cln1∆ cln2∆ cln3∆ cdh1∆
- GAL-SIC1 cln1∆ cln2∆ cdh1∆
- GAL-SIC1 GAL-CLN2 cln1∆ cln2∆ cdh1∆
- CLB1 clb2∆ cdh1∆
- GAL-CLB2 cdh1∆
- GAL-CLB5 cdh1∆
- cdc14-ts cdh1∆
- cdc15∆ net1-ts cdh1∆
- APC-A cdh1∆
- APC-A cdh1∆ in galactose
- APC-A cdh1∆ GAL-SIC1
- APC-A cdh1∆ GAL-CDC6
- APC-A cdh1∆ multi-copy SIC1
- APC-A cdh1∆ multicopy CDC6
- APC-A cdh1∆ multicopy CDC20
- Cdh1 constitutively active
cdh1∆
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Simulation:
Change of parameters: kscdh=0, init CDH1T=CDH1=0.
Length of G1 phase: 66.3 min.
Mass at division: 1.91
Experiments:
Schwab, M., Lutum, A.S. and Seufert, W. (1997). Yeast Hct1 is a regulator of Clb2 cyclin proteolysis. Cell 90:683-693.
[Abstract] [Article]
[Abstract] [Article]
Jorgensen, P., Nishikawa, J.L., Breitkreutz, B.J. and Tyers, M. (2002). Systematic identification of pathways that couple cell growth and division in yeast. Science 297:395-400.
[Abstract] [Article]
[Abstract] [Article]
Wasch, R. and Cross, F. (2002). APC-dependent proteolysis of the mitotic cyclin Clb2 is essential for mitotic exit. Nature 418:556-562.
[Abstract] [Article]
[Abstract] [Article]
Experimental results: Schwab and Cross: Viable, Clb2 level high throughout the cell cycle.
Jorgensen: Fig. 2 & Table 1. cdh1∆ mutant is viable but smaller than WT. It is born at a smaller size (24 fL for WT and 14fL for cdh1∆), it grows slower (MDT is 87 min for WT and 115 min for the mutant), and buds at a smaller size (the critical size for budding is 32 fL for WT and 27 fL for the mutant).
Jorgensen: Fig. 2 & Table 1. cdh1∆ mutant is viable but smaller than WT. It is born at a smaller size (24 fL for WT and 14fL for cdh1∆), it grows slower (MDT is 87 min for WT and 115 min for the mutant), and buds at a smaller size (the critical size for budding is 32 fL for WT and 27 fL for the mutant).
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Slower growth rate indicates some effect of Cdh1 on nutrient uptake or proteinsynthesis, which the model does not consider. Early budding of cdh1∆ cells suggests that Cdh1 is inhibitory for START: it may target some yet-unidentified activator of START for ubiquitin-dependent proteolysis. The known Cdh1 targets (Clb2, Cdc20, Cdc5) do not satisfy this requirement, they are all inhibitors START: Clb2 turns off SBF, Cdc20 degrades Clb5, and Cdc5 activates Cdc14 release, which in turn activates Sic1 synthesis.