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Summary: Molecular Cell
Article
Robust Control of Nitrogen Assimilation
by a Bifunctional Enzyme in E. coli
Yuval Hart,1,3 Daniel Madar,1,3 Jie Yuan,2,3 Anat Bren,1 Avraham E. Mayo,1 Joshua D. Rabinowitz,2 and Uri Alon1,*
1Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel
2Lewis-Singer Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544, USA
3These authors contributed equally to this work
*Correspondence: urialon@weizmann.ac.il
DOI 10.1016/j.molcel.2010.12.023
SUMMARY
Bacteria regulate the assimilation of multiple nutri-
ents to enable growth. How is balanced utilization
achieved, despite fluctuations in the concentrations
of the enzymes that make up the regulatory circuitry?
Here we address this question by studying the
nitrogen system of E. coli. A mechanism based on
the avidity of a bifunctional enzyme, adenylyltrans-
ferase (AT/AR), to its multimeric substrate, glutamine
synthetase, is proposed to maintain a robust ratio
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