Thought questions

Thought questions - NEW JERSEY DOUCHEBAGS Thought question:...

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Thought question: Why do you suppose that phosphorylation / dephosphorylation, as opposed to allosteric binding of small molecules, plays such a prominent role in switching proteins on and off in signaling pathways ? However, at the receptor level allosteric interactions are common. Allosteric interactions take longer Phosphorylation/dephosphorylation is faster and not as regulated Signal regulated by allosteric signaling; Already passed and been okay to pass through the cell and been okayed to carry on its functions; then going for speed, not looking to regulate looking to send the signal quickly Kinase phosphorlaytion causes activation; many protein may be activated but only the target cell protein matter Many MAPKs are activated by the same pathogen but are associated with signal transduction for different signaling hormones. To add to the complexity of the problem in Arabidopsis there are 60 MAPKKK (3K), 10 MAPKK (2K) and 20 MAPK (1K). How is specificity of the appropriate response maintained with such a truncated distribution of Kinase genes. What are the advantages of having this type of system? Advantages: a larger, and more responses possible; different combinations; certain signals code for certain MAPK in the 3K; combinations lead to different transcription factors; able to control that; each would give you a different response but those responses are specific. Negative feedback; when you get to the kinases doesn’t just automatically phosphoralyate you can control it. One pathogen activates many different pathways; could work like a signal transduction; each signal codes for a different response. Each give each other a specific response. By giving many different signals your giving one specific signal
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This note was uploaded on 04/20/2010 for the course BIOL 4064 taught by Professor Dr.reyna during the Spring '09 term at Ouachita Baptist.

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Thought questions - NEW JERSEY DOUCHEBAGS Thought question:...

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