Date Approved

9-8-2025

Embargo Period

9-8-2025

Document Type

Dissertation

Degree Name

Ph.D. Biological and Biomedical Sciences

Department

Biological and Biomedical Sciences

College

College of Science & Mathematics

Advisor

Jason Heindl, Ph.D.

Committee Member 1

Maggie Pearce, Ph.D.

Committee Member 2

Svjetlana (Lana) Vojvodic Kruse, Ph.D.

Committee Member 3

Bela Peethambaran, Ph.D.

Committee Member 4

Amy T. Ma, Ph.D.

Committee Member 5

Vincent Tam, Ph.D.

Disciplines

Life Sciences | Microbiology

Abstract

Cyclic diguanylate monophosphate (c-di-GMP) is a second messenger that is responsible for attachment and motility in many prokaryotic systems and controls the signaling pathway for the motile to sessile transition in many bacteria. Many c-di-GMP-metabolizing proteins are diguanylate cyclases (DGCs), responsible for the synthesis of c-di-GMP and characterized by a c-di-GMP synthesizing domain, e.g., GGDEF domain. Other c-di-GMP-metabolizing proteins contain c-di-GMP degradative domains, e.g., EAL, characterized by phosphodiesterase activity (PDE). In Agrobacterium tumefaciens, out of 31 predicted proteins regulating the c-di-GMP level, this project focuses on the predicted dual-function DGC/PDE, DcpB. We hypothesized that DcpB plays a role in the overall metabolism of c-di-GMP and affects biofilm formation and motility. Overall, our results suggest that DcpB is a c-di-GMP metabolizing protein, resulting in cell cycle-dependent control of motility and biofilm formation in A. tumefaciens, most likely functioning as a cell cycle-dependent PDE under our experimental conditions.

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