In the last 20 years, a growing army of systems biologists has employed quantitative experimental methods and theoretical tools of data analysis and mathematical modeling to unravel the molecular details of biological control systems with novel studies of biochemical clocks, cellular decision-making, and signaling networks in time and space. Few people know that one of the roots of this new paradigm in cell biology can be traced to a serendipitous discovery by an obscure Russian biochemist, Boris Belousov, who was studying the oxidation of citric acid. The story is told here from an historical perspective, tracing its meandering path through glycolytic oscillations, cAMP signaling, and frog egg development. The connections among these diverse themes are drawn out by simple mathematical models (nonlinear differential equations) that share common structures and properties.
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In this issue Love and colleagues (pp. 207–223) determine the atomic structure and define the enzymatic function of Escherichia coli O157:H7 phage FTEBc1 endolysin, LysT84. Overall, their study supports rational engineering of related endolysins into effective antibacterial agents. The cover image shows the peptidoglycan binding domain of LysT84 (purple) superimposed with the domains of AP3gp15 (blue) and fKZgp144 (brown) shows the three α-helix bundle architecture is conserved. The image is courtesy of Renwick Dobson.
From the Belousov–Zhabotinsky reaction to biochemical clocks, traveling waves and cell cycle regulation
John J. Tyson; From the Belousov–Zhabotinsky reaction to biochemical clocks, traveling waves and cell cycle regulation. Biochem J 28 January 2022; 479 (2): 185–206. doi: https://doi.org/10.1042/BCJ20210370
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