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Characterization of the affects of specialized acyl carrier proteins on unusual LPS-hydroxy fatty acids in Geobacter metallireducens


EMSL Project ID
44700

Abstract

Many bacteria have specialized acyl carrier proteins (ACPs) that are involved in synthesis of diverse lipopolysaccharides (LPS). Diversity within LPS aids in survival of Gram-negative bacteria in various environments and is one of the major virulence factors in Gram-negative pathogens. Very little is known about the altered acylation patterns of LPS due to specialized ACPs. In order to determine the effects of the specialized ACPs on LPS-hydroxy fatty acids, (OH-FAs) in G. metallireducens, we will use mass spectrometry to characterize the LPS OH-FAs after knockout of the two specialized ACPs, GmACP2 and GmACP3. Preliminary work will be done on G. metallireducens that have been transformed with plasmids for overexpression of these proteins. In addition, NMR characterization of apo- and holo- ACPs will be used to better understand the relationship between the structure and dynamics of these proteins and their ability to recognize the specific set of proteins involved in LPS modification.

Project Details

Project type
Large-Scale EMSL Research
Start Date
2011-10-01
End Date
2014-09-30
Status
Closed

Team

Principal Investigator

Theresa Ramelot
Institution
Miami University

Team Members

Aaron Peacock
Institution
SPAWAR Systems Command Atlantic

Pier-Luc Tremblay
Institution
University of Massachusetts Amherst

Philip Long
Institution
Lawrence Berkeley National Laboratory

Derek Lovley
Institution
University of Massachusetts Amherst

Gaetano Montelione
Institution
Rutgers University

Michael Kennedy
Institution
Miami University

Related Publications

Ramelot TA, PM Rossi, F Forouhar, HW Lee, Y Yang, S Ni, S Unser, S Lew, J Seetharaman, R Xiao, T Acton, JK Everett, JH Prestegard, JF Hunt, G Montelione, and MA Kennedy. 2012. "Structure of a Specialized Acyl Carrier Protein Essential for Lipid A Biosynthesis with Very Long-chain Fatty Acids in Open and Closed Conformations." Biochemistry 51(37):7239-7249. doi:10.1021/bi300546b