BIOL201 Lecture Notes - Lecture 18: S Phase, Anaphase-Promoting Complex, Telophase

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amethystyak344

22 Jan 2016

School

University of Alberta

Department

Biology (Biological Sciences)

Course

BIOL201

Professor

Warren Gallin

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Document Summary

Cell size: important to reach the appropriate size. * when conditions are met, also need high concentration of mitotic cyclin. Only when the cyclin activity was highest then there was mpf activity which is a main regulator of mitosis. Cyclin concentration increases linearly over time, yet the mpf activity is coming in waves and only occurs at highest concentration of cyclin. This then drives the cell into mitosis out of g2. The mitotic cdk activity is regulated by wee1, a kinase, and by cdc25, a phosphatase. When the wee1 and cdc25 activity levels are adjusted away from normal, the yeast daughter cell size is affected: two inhibitory phosphate groups are attached to the cdk molecule by inactive complex. enzymes- inhibiting kinases. High wee1 and low cdc25- cells get longer. Have kinase and phosphatase (they always go in opposite directions). First suggestion that wee1 and cdc25 may have opposing activities.

Related Questions

QUESTION 1:

(a)Examine the Figure below relating to the S.pombe cellcycle:

1) Describe the function of Cdc25 and Wee1and why deficit of Cdc25 or excess of Wee1 can cause G2arrest

2) b) Describe how deficit of Wee1 or excess ofCdc25 may result in abnormally small cells

(b) Theactivities of Wee1 tyrosine kinase and Cdc25 tyrosine phospatasedetermine the state of phosphorylation of tyrosine 15 in the Cdk1component of mitotic cyclin-Cdk complexes (MPF). When tyrosine 15is phosphorylated, M-Cdk is inactive; when tyrosine 15 is notphosphorylated, M-Cdk is active. Just as the activity of M-Cdkitself is controlled by phosphorylation, so too are the activitiesof Wee1 kinase and Cdc25 phosphatase. The regulation of thesevarious activities can be studied in extracts of frog oocytes. Insuch extracts Wee1 tyrosine kinase is active and Cdc25 tyrosinephosphatase is inactive. As a result M-Cdk is inactive because itsCdk1 component is phosphorylated on tyrosine 15. M-Cdk in theseextracts can be rapidly activated by addition of okadaic acid,which is a potent inhibitor of serine/threonine phosphatases. Usingantibodies specific for each component it is possible to examinetheir phosphorylation states by changes in mobility upon gelelectrophoresis.

(Phosphorylated proteins generally run slower than theirnon phosphorylated counterparts).

1) Based on theresults with okadaic acid, decide whether the active forms of Wee1and Cdc25 are phosphorylated or unphosphorylated. In the figureindicate the phosphorylated forms of Wee 1 and Cdc25 and label thearrows connecting their active and inactive forms to show whichtransitions are controlled by protein kinases and which by proteinphosphatases.

2) Are the proteinkinases and phosphatases that control Wee1 and Cdc25 specific forserine/threonine side chains or for tyrosine side chains? How doyou know?

3) How doesaddition of okadaic acid cause an increase in phosphorylation ofWee1 and Cdc25, but a decrease in phosphorylation ofCdk1?

4) If you assumethat Cdc25 and Wee1 are targets for phosphorylation by activeM-Cdk, can you explain how the appearance of a small amount ofactive M-Cdk would lead to its rapid and completeactivation?

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BIOL201 Lecture Notes - Lecture 18: S Phase, Anaphase-Promoting Complex, Telophase

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