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RAJESH S. GOKHALE, Ph.D.
Chemical
Biology Group
National
Aruna Asaf Ali Marg
+91-11-26703761
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Scientist, National Institute of
Immunology
Faculty Member (Honorary), Jawaharlal
Nehru Centre for Advanced Scientific Research
HHMI International Research Scholar
M.Sc., 1990, Indian Institute of Technology,
Ph.D., 1996, Indian Institute of Science,
Postdoctoral Fellow, 1996-1999,
Wellcome Trust Senior Research Fellowship in
Biomedical Science 2001-2006
B. M. Birla
Science Prize, 2003
Swarnajayanti Fellowship, 2006-2011
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My research group is interested to address problems related to metabolic diversity and complexity. In this multidisciplinary program engaged at the interface of chemistry, biochemistry, and structural and molecular biology, we are elucidating the biochemical pathways leading to the assembly of various metabolites. Our studies, in general, should identify mechanisms that facilitate generation of metabolic repertoire in nature by using limited set of genes.
Chemical Biology of Mycobacterium Tuberculosis
The
microbial genome sequencing projects have revealed an unanticipated variety of
metabolic and cellular capabilities. It
is therefore not surprising that microbes can successfully adapt to different
habitats successfully. M.
tuberculosis has been a successful pathogen and the key to its success lies
in its ability to reside and proliferate inside host macrophage despite the
antimicrobial properties of these cells.
Pathogenic mycobacteria
are endowed with remarkable cell envelope of fascinating molecular
architecture. Along with complex lipids
and polysaccharides, mycobacterial cell envelope is
associated with numerous proteins that influence cellular structure and its
interactions with host cells. Despite
considerable progress in characterization of the major cellular components of M.
tuberculosis, there is little information on the nature of proteins
associated with the cell envelope. Since
the cell envelope constitutes the key interface between pathogen and host, the
cell wall-associated proteins and lipids are presumable key determinants of
pathogenesis and immunogenicity. There is mounting
evidence that despite the lack of significant genetic heterogeneity
between strains of M. tuberculosis, the variable expression leading to
phenotypic heterogeneity contributes towards virulence and persistence of this
major killer of humankind. We are
interested in dissecting the molecular mechanisms that generate functional
diversity through “enzymatic crosstalk" that will provide insight into
mechanisms employed by pathogens to generate metabolite diversity.
Functional Significane
of Polyketide Synthases in Dictyostelium Disscodium
Dictyostelium genome has revealed
a very large number of genes homologous to polyketide
synthases (PKSs). Although the functional significance of these
genes is not known, some of the metabolites that could be biosynthesized by PKSs have been characterized and their role in
differentiation has been demonstrated.
The advances in the understanding of the biochemical basis for the
programming of the polyketide biosynthesis provide an
impetus and opportunity to dissect the roles of these enzymes from these
versatile soil amoebae.
Dissecting
Biochemical Mechanisms of the Melanocyte and Melanin Disappearnce in Vitiligo
The advances in neural crest cell
culture and the availability of human genome sequence presents a tantalizing
opportunity to carry out a multi-disciplinary study to dissect the integrated
roles of different causal factors involved in the genesis of vitiligo. Moreover,
the manifestation of this disease on the skin surface provides a relatively
easy access to affected cells/tissues.
In this study we are investigating into the biochemical mechanisms
underlying melanin and melanocyte disappearance in vitiligo by combination of hypothesis-driven and
exploratory research.
Significant Publications
(Since 2003)
1.
Krithika R.,
2.
Arora P., Vats A., Saxena
P., Mohanty D., Gokhale R.S. (2005) Promiscuous fatty acyl-CoA
ligases produce acyl-CoA
and acyl-SNAC precursors for polyketide
biosynthesis. J. Am. Chem. Soc. 127(26):9388-9.
3.
Trivedi O.A., Arora
P., Vats A., Ansari M.Z., Tickoo
R., Sridharan V., Mohanty
D., Gokhale, R.S. (2005) Dissecting the mechanism
and assembly of a complex virulence mycobacterial
lipid. Mol Cell 17(5):631-43.
4.
Sankarnarayanan R.*, Saxena P., Marathe U.B., Gokhale R.S.*, Shanmugam
V. M., Rukmini R. (2004) A novel substrate binding
tunnel in mycobacterial type III polyketide
synthase reveals structural basis for generating
diverse metabolites. Nat Struct Mol Biol.
11(9):894-900. (* represents corresponding authors).
5.
Trivedi O.A., Arora
P., Sridharan V., Tickoo
R., Mohanty D., Gokhale, R.S. (2004) Enzymic activation and
transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428 (6981),
441-445.
6.
Saxena P., Yadav G., Mohanty D., Gokhale R.S.
(2003): A New Family of Type III Polyketide Synthases in Mycobacterium tuberculosis. J.
Biol. Chem. 278(45), 44780-44790.
Present
Group Members
