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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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