David S. Weiss, PhD


Associate Professor of Microbiology

Contact Information

Office: 3-372 Bowen Science Building
51 Newton Rd
Iowa City, IA 52242
Phone: 319-335-7785

Lab: 3-303 Bowen Science Building
51 Newton Rd
Iowa City, IA 52242
Phone: 319-335-7944

Email: david-weiss@uiowa.edu
Web: Weiss Lab Website


BA, Biology , Swarthmore College
PhD, Microbiology, University of California, Berkeley

Post Doctorate, Microbiology, Max Planck Institute for Terrestrial Microbiology
Post Doctorate, Microbiology, Harvard Medical School

Education/Training Program Affiliations

Department of Microbiology Graduate Program
Interdisciplinary Graduate Program in Genetics

Research Summary

Background: We use bacteria as model organisms for addressing one of the most fundamental problems in cell biology -- How do cells divide? More specifically, we want to know how the division septum is formed and how its formation is regulated. Another objective is to understand how proteins are targeted to specific subcellular sites, especially how cell division proteins localize to the midcell.

Recent Results: We have approached these issues by screening for and/or characterizing new cell division proteins of Escherichia coli. This led to the identification of three new division proteins named DamX, DedD and RlpA. All three proteins contain a C-terminal "SPOR" domain that binds to the peptidoglycan cell wall. Surprisingly, we found that the SPOR domain alone is able to localize to the midcell. We think SPOR domains must be binding to a special peptidoglycan form (or structure) in the division septum. Figuring out what that structure is might provide important new insights concerning peptidoglycan synthesis during cell division.

Future Directions: The questions we are addressing now include: What sequences in SPOR domains specify septal localization? What is the unique feature of septal peptidoglycan that SPOR domains recognize? What role do the SPOR domain proteins play in cell division? What are the roles of SPOR domain proteins in other bacteria? In this regard, it is important to note that SPOR domain proteins are found in hundreds of bacterial species, including many important pathogens.

Significance: A better understanding of cell division and protein localization in E. coli might shed light on these processes in other organisms. In addition, our studies might lead to more knowledge-based approaches to developing new antibiotics.

Center, Program and Institute Affiliations

Center for Biocatalysis and Bioprocessing

Selected Publications

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Yahashiri A, Jorgenson M, Weiss D.  Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides.  Proc Natl Acad Sci U S A.  2015 September 8. 112(36):11347-52.

Weiss D.  Last but not least: new insights into how FtsN triggers constriction during Escherichia coli cell division.  Mol Microbiol.  2015 March. 95(6):903-9.

Ransom E, Ellermeier C, Weiss D.  Use of mCherry Red fluorescent protein for studies of protein localization and gene expression in Clostridium difficile.  Appl Environ Microbiol.  2015 March. 81(5):1652-60.

Jorgenson M, Chen Y, Yahashiri A, Popham D, Weiss D.  The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation in Pseudomonas aeruginosa.  Mol Microbiol.  2014 July. 93(1):113-28.

Ransom E, Williams K, Weiss D, Ellermeier C.  Identification and Characterization of a Gene Cluster Required for Proper Rod Shape, Cell Division, and Pathogenesis in Clostridium difficile.  J Bacteriol.  2014 June 15. 196(12):2290-300.

Söderström B, Skoog K, Blom H, Weiss D, von Heijne G, Daley D.  Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization.  Mol Microbiol.  2014 April. 92(1):1-9.

Duncan T, Yahashiri A, Arends S, Popham D, Weiss D.  Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN.  J Bacteriol.  2013 December. 195(23):5308-15.

Williams K, Yahashiri A, Arends S, Popham D, Fowler C, Weiss D.  Nuclear Magnetic Resonance Solution Structure of the Peptidoglycan-Binding SPOR Domain from Escherichia coli DamX: Insights into Septal Localization.  Biochemistry.  2013 January 4. 52(4):627-39.

Gode-Potratz C, Kustusch R, Breheny P, Weiss D, McCarter L.  Surface sensing in Vibrio parahaemolyticus triggers a programme of gene expression that promotes colonization and virulence.  Mol Microbiol.  2011 January. 79(1):240-63.

Arends S, Williams K, Scott R, Rolong S, Popham D, Weiss D.  Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA.  J Bacteriol.  2010 January. 192(1):242-55.

Date Last Modified: 06/06/2016 - 13:17:48