Queuosine salvage in Bartonella henselae Houston 1: a unique evolutionary path

Author:

Quaiyum Samia1,Yuan Yifeng1,Sun Guangxin2,Ratnayake R. M. Madhushi N.34,Hutinet Geoffrey51,Dedon Peter C.2ORCID,Minnick Michael F.6,de Crécy-Lagard Valérie71ORCID

Affiliation:

1. Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611, USA

2. Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA

3. Present address: Department of Biochemistry, School of Medicine, Vanderbilt University, Nashville, TN 37232, USA

4. Department of Chemistry, University of Florida, Gainesville, FL 32611, USA

5. Present address: Department of Biology, Haverford College, 370 Lancaster Ave., Haverford, PA, USA

6. Division of Biological Sciences, University of Montana, Missoula, Montana, MT 59812, USA

7. Genetic Institute, University of Florida, FL 32611, USA

Abstract

Graphical Abstract The substrate specificity of bacterial TGT and Q precursor transporter protein shifts from preQ1 to the queuine base in intracellular human pathogens such as Chlamydia trachomatis, driven by adaptation to the intracellular environment. The facultative intracellular pathogen Bartonella henselae exhibits a rare dual-substrate specificity for these Q salvage enzymes that represents an evolutionary transition state.

Funder

National Institute of General Medical Sciences

National Institute of Environmental Health Sciences

National Research Foundation of Singapore

Publisher

Microbiology Society

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