Background: Cell function necessitates the assemblage of proteins into complexes, a process which requires further regulation on top of the fairly understood mechanisms used to control the transcription and translation of a single protein. However, not much is known about how protein levels are controlled to realize that regulation. Results: We integrated data on the composition of yeast protein complexes and the dynamics of their protein building-blocks concentrations to show how the cell regulates protein levels to optimize complex formation. We find that proteins which are subunits of the same complex tend to have similar levels which change similarly following a change in growth conditions, and that abundant proteins undergo larger decrease in their copy number when grown in minimal media. We also study the fluctuations in protein levels and find them to be significantly smaller in large complexes, and in the least abundant subunit of each complex. We use a mathematical model of complex synthesis to explain how all these observations increase the efficiency of complex synthesis, in terms of better utilization of the available molecules and better resilience to stochastic variations. Conclusion: In conclusion, these results indicate an intricate regulation at all levels of protein production for the purpose of optimizing complex formation.
Bibliographical noteFunding Information:
We thank the Israel Science Foundation and the Israel Center for Complexity Science for financial support, and S. Havlin for discussions. We also thank anonymous referees for many helpful comments. SC is supported by the Adams Fellowship Program of the Israel Academy of Sciences and Humanities. EYL is supported by the Machiah foundation of the Jewish community endowment fund.