التفاصيل البيبلوغرافية
| العنوان: |
Protein-Protein Interaction Affinity Plays a Crucial Role in Controlling the Sho1p-Mediated Signal Transduction Pathway in Yeast |
| المؤلفون: |
Marles, Jennifer A.1, Dahesh, Samira2, Haynes, Jennifer2, Andrews, Brenda J.2, Davidson, Alan R.1,2 alan.davidson@utoronto.ca |
| المصدر: |
Molecular Cell. Jun2004, Vol. 14 Issue 6, p813-823. 11p. |
| مصطلحات موضوعية: |
*PROTEIN-protein interactions, *MOLECULAR association, *GENETIC transduction, *YEAST, *MICROBIAL genetics |
| مستخلص: |
Protein-protein interactions are required for most cellular functions, yet little is known about the relationship between protein-protein interaction affinity and biological activity. To investigate this issue, we engineered a series of mutants that incrementally reduced the affinity of the yeast Sho1p SH3 domain for its in vivo target, the MAP kinase kinase Pbs2p. We demonstrate a strong linear correlation between the binding energy of these mutants and quantitative in vivo outputs from the HOG high-osmolarity response pathway controlled by Sho1p. In addition, we find that reduction in binding affinity for the correct target within this pathway causes a proportional increase in misactivation of the related mating pheromone response pathway and that strong binding affinity alone does not guarantee efficient biological activity. Our experiments also indicate that a second binding surface on the Sho1p SH3 domain is required for its proper in vivo function. [Copyright &y& Elsevier] |
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