Structure and function of FtsZ and interacting protein partners in cell division of agrobacterium tumefaciens
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[EMBARGOED UNTIL 12/01/2025] Our understanding of bacterial cell division arises from research spanning over five decades of research from multidisciplinary approaches including genetics, biochemistry, cell biology, biophysics, and computational modeling. While the goal of most of this prior research has been to identify key players in bacterial cell division, most of our current understanding of cell division in diderm bacteria is based on research focused on Escherichia coli, a Gammaproteobacteria. The model of cell division built off the E. coli work is expansive and describes tens of core proteins critical for cell division, as well as a myriad of accessory proteins. Recent exploration of cell division in other diderm bacteria reveals that a summative model derived from E. coli is not sufficient. In this dissertation, we detail unique features for bacterial cell division found in Alphaproteobacterial members. Specifically, we focus on duplications of FtsZ, expansion of FtsZ C-Terminal Linker (CTL) domains, and the function of FzlA, a clade-specific FtsZ binding partner. Chapter 1, provides an overview comparing features involved in cell division in three diderm bacteria, E. coli, Caulobacter crescentus, and Agrobacterium tumefaciens, before introducing notable features of the predicted A. tumefaciens model that is explored in this dissertation. In chapter 2, we discuss FtsZ duplications and present our findings on toxicity induced by overexpression of FtsZ1. Chapter 3 explores the expansion of CTL domains in FtsZ proteins across the Alphaproteobacterial class, with a comprehensive analysis of the CTL function in A. tumefaciens. In chapter 4, we describe the Alphaproteobacterial FtsZ-binding partner FzlA and its functions in A. tumefaciens, in chapter 4. We conclude with chapter 5 by providing a summary of the contributions made to the field throughout this dissertation work.
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Ph. D.