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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