Cell cycle 2 Flashcards

1
Q

S phase

A

dna replication and chromosome duplication

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2
Q

M phase

A

mitosis and cytokinesis

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3
Q

Cell cycle control system

A

Cyclically activated cyclin dependant protein kinases

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4
Q

Whats a cyclin-cdk complex formed off

A

cyclin activates cdk.

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5
Q

G1 cyclins

A

Cyclins bind and activate cdks, stimulate entry into a new cell, concentration depends on rate of cell growth

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6
Q

S cyclins

A

Cyclins that activate cdk for dna synthesis, remains high in S phase

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7
Q

M cyclins

A

Cyclins that activate CDKS for mitosis, peaks in metaphase

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8
Q

What does cyclin do other than activate CDKs?

A

directs the complex to specific target proteins, phosphorylating different substrate proteins

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9
Q

Explain how CDK can become active through cyclin activation

A

In inactive state, T loop blocks active site. Once cyclin binds to CDK T loop structure changes and CDK becomes active as cyclin binds to it

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10
Q

Explain mechanism of wee1 and cdc25 regulatory pathway

A

Active CDK complex can be inhibited by further phosphorylation in active site. Phosphorylation of try is by wee1
Cdc25 can dephosphorylate this site and lead to activation

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11
Q

Explain how CDK inhibitor proteins affect binding of cyclin

A

CKL is an inhibitor protein which binds to the active site of CDK, making binding of cyclin not possible.

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12
Q

Explain role of RB and e2f

A

RB is a tumour supressor protein that prevents uncontrolled cell proliferation
E2F is a transcription factor that controls expression of genes essential for DNA synthesis

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13
Q

Explain process of growth factors leading to production of CDK and cyclin complex and effect the complex has on RB and E2F

A

in early G1 phase a growth factor leads to RAS pathway which stimulates formation of CDK and cyclin, this complex phosphorylates RB, causing a conformational change, leading to e2f being freed and gene expression continuing.

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14
Q

Whats the role of the Ubiquitin pathway

A

essentially leads to degradation of specific proteins in a chain of reactions

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15
Q

Whats the main role of ubiquitin

A

It targets a protein that needs to be degraded via a proteosome

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16
Q

What is a proteosome

A

a large protein complex which degrades polyubiquated proteins

17
Q

how do proteosomes work

A

they recognize proteins marked by a polyubiquitin chain, ubiquitin is recycled at an early stage.

18
Q

Explain translocation mechanism

A

protein is translocated into proteosome core, where ATPases unfold substrate protein, a hyrolyse cleaves ubiquitin from protein, where it is recycled.

19
Q

Explain role of E1

A

Ub activating enzyme

20
Q

Explain role of E2

A

is the conjugating enzyme, where UB is transferred from E1 to E3

21
Q

Explain role of E3

A

attatches UB to target protein, making protein ready to be detected by proteosome

22
Q

What is the APC

A

Anaphase promoting complex: is a large E3 ubiquitin ligase complex, which ligases ubiquitin to a target protein

23
Q

Explain role of the APC

A

Promotes transition from metaphase to anaphase , targeting proteins for degradation.

24
Q

What is securin

A

is tagged for degredation, allows seperase to cleave cohesins, enabling sister chromatid seperation

25
Q

What happens to cyclins

A

they are degraded, and inactivated

26
Q

How is the APC activated

A

via co activators, cdc20 activates APC during metaphase to anaphase transition

27
Q

how does cdh1 play a role

A

maintains APC during M phase and G1