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OJBTM
Online Journal of Bioinformatics

 

Volume 13(1):14-26, 2012


In silico horizontal gene transfer and functional motif in GshF protein of Listeria monocytogenes

 

Vanishree Srinivas1 MSc MPhil, Juergen Kreft2 MSc PhD, Shubha Gopal1 MSc PhD.

 

1Department of Microbiology, University of Mysore, Manasagangotri, Mysore - 570 006, Karnataka, India. 2Department of Microbiology, Biocenter, University of Wuerzburg, 97074 Wuerzburg, Germany

 

ABSTRACT

 

Srinivas V, Kreft J, Gopal S., In silico horizontal gene transfer and functional motif in GshF protein of Listeria monocytogenes, Online J Bioinform, 13(1):14-26, 2012. Glutathione synthesis, a two step process in Listeria monocytogenes, is performed by a single Glutathione fusion protein (GshF). GshF comprises 776 amino acids with N terminal gammaglutamylcysteine ligase (GshA) and C terminal ATP grasp dependent domains. Amino acids 338 to 580 were horizontally gene transferred through a symbiotic relationship within the host and other bacteria. Flipping of unstructured proteins in eukaryotes during host pathogen interaction may have triggered fusion. In this study, a novel motif KPKX|S/T|TN in L. monocytogenes EGDe was identified in GshF/GshAB (Glutathione biosynthesis bifunctional protein) conserved in proteobacteria, bacteriodetes and firmicutes. The motif was present in the B-loop and residues were exposed. L. monocytogenes EGD-e motif consisted of phosphorylation residues which could regulate ligase activity.

 

Keywords: In silico analysis, GshF protein, Phylogeny, Gene fusion, Listeria


 

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