enzyme (Tyr 15 of phorylated, the en- -ylation state of any lows replication. The role of Cdk inhibitors in mammalian cells is discussed on page 581. Mitosis rphase (G,) Interphase (G,) Thr161- P Tyr15- P Thr161- P CAK Weel Cdc25 cdc2 kinase cdc2 kinase cdc2 kinase G, fission yeast cell Post-mitotic fission yeast cells Cyclin Cyclin Cyclin Inactive Inactive Active Cyclin Degradation Wild type sion yeast cell cycle phorylation of critical nicrograph of wild interacts with a G2 weel- G2 of phosphorylation of a Veel (step 1). A sepa- another residue (Thr W

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The figure below details a pathway in yeast involving kinases and a phosphatase and the regulation of a specific cyclin-cdk complex. CAK kinase controls the phosphorylation of Thr161. The phosphorylation of Tyr15 is controlled by Wee1 and Cdc25.  In this problem, focus on the phosphorylation of Tyr15 by  Wee1 and Cdc25.   

1. If Wee1 kinase was inactive, what would happen to the cyclin-cdc2 complex?

                 Would the cells enter mitosis and divide more or less often?

                  Would the cells end up being smaller or larger than normal?

2. If Cdc25 phosphatase was inactive, what would happen to the cyclin-cdc2 complex?

                  Would the cells enter mitosis and divide more or less often?

                  Would the cells end up being smaller or larger than normal?  

OF mitotic
residue in the ATP-binding pocket of the enzyme (Tyr 15 of
edc2 in Figure 14.66). If this residue is phosphorylated, the en-
vyme is inactive, regardless of the phosphorylation state of any
lows the cyclin-Cdk that is present in the cell to
replication. The role of Cdk inhibitors in mammalian cells is
discussed on page 581.
Mitosis
Interphase (G,)
Interphase (G,)
Thr161- P
Tyr15- P
Thr161-P
NAD BIOU
CAK
Weel
Cdc25
cdc2
kinase
cdc2
kinase
cdc2
kinase
cdc2
kinase
ontain
Post-mitotic fission
G, fission
yeast cell
Inactive
Cyclin
Cyclin
Cyclin
Inactive
yeast cells
Inactive
Active
Cyclin
he chromo
from inter
during the
pambar su
Degradation
(9)
Wild type
Figure 14.6 Progression through the fission yeast cell cycle
requires the phosphorylation and dephosphorylation of critical
ede2 residues. (a) Colorized scanning electron micrograph of wild type
fission yeast cells. (b) During G, the cdc2 kinase interacts with a
mitotic cyclin but remains inactive as the result of phosphorylation of a
key tyrosine residue (Tyr 15 in fission yeast) by Wee1 (step 1). A sepa-
ate kinane, called CAK, transfers a phosphate to another residue (Thr
W
Exit from
weel-
W
uo pasna
Transcribed Image Text:OF mitotic residue in the ATP-binding pocket of the enzyme (Tyr 15 of edc2 in Figure 14.66). If this residue is phosphorylated, the en- vyme is inactive, regardless of the phosphorylation state of any lows the cyclin-Cdk that is present in the cell to replication. The role of Cdk inhibitors in mammalian cells is discussed on page 581. Mitosis Interphase (G,) Interphase (G,) Thr161- P Tyr15- P Thr161-P NAD BIOU CAK Weel Cdc25 cdc2 kinase cdc2 kinase cdc2 kinase cdc2 kinase ontain Post-mitotic fission G, fission yeast cell Inactive Cyclin Cyclin Cyclin Inactive yeast cells Inactive Active Cyclin he chromo from inter during the pambar su Degradation (9) Wild type Figure 14.6 Progression through the fission yeast cell cycle requires the phosphorylation and dephosphorylation of critical ede2 residues. (a) Colorized scanning electron micrograph of wild type fission yeast cells. (b) During G, the cdc2 kinase interacts with a mitotic cyclin but remains inactive as the result of phosphorylation of a key tyrosine residue (Tyr 15 in fission yeast) by Wee1 (step 1). A sepa- ate kinane, called CAK, transfers a phosphate to another residue (Thr W Exit from weel- W uo pasna
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