gototopgototop

Main Menu

Name:
Dr. S. Kumaran
Expertise:
Biology of Macromolecular Assemblies

Contact Address:

E-mail: skumaran@imtech.res.in
Ph: 91-172-2636680-94   Ext: 3283
Fax:91-172-2690585
Dr. S. Kumaran, Scientist
Institute of Microbial Technology
Sector 39-A
Chandigarh, 160036, India

Write-up of research and development interests/focus, past and present goals:

Current Research

My lab is interested in synthesizing the knowledge of assembly, structure, and regulatory mechanisms of macromolecular assemblies that form biological circuits. We use the knowledge of biology, chemistry, and physics to understand the regulatory strategies of macromolecular assemblies and define their physiological role in the cell. Our goals will be achieved using a variety of techniques including molecular biology, cell biology, X-ray crystallography, analytical ultracentrifugation, isothermal titration calorimetry (ITC), fluorescence & CD spectroscopy, mass spectrometry, surface plasma resonance, light scattering, steady state & pre-steady state kinetic approaches, and computational methods.

Assembly, structure, and regulatory strategies of multi-enzyme complexes

We study the regulatory protein-protein & protein-ligand interactions in cysteine synthase, a multi-enzyme complex from pathogenic bacteria. Our goal is to understand the structure, energetics, and kinetics of such interactions and physiological significance of these interactions in order to interfere rationally with small molecules for therapeutic purposes.

Assembly & Regulation of Transcriptional Regulatory Complexes (TRC’s)

Bacterial transcriptional regulators play a vital role in virulence, pathogenicity, symbiosis, and survival. The assembly of functional transcriptional regulatory complex (TRC) requires a highly coordinated sequential set of events among the components of TRC. Our studies are aimed at understanding the regulatory principles of assembly of functional TRC which dictates the frequency of transcription of genes. We hope to provide a physical, mechanical and physiological basis of regulation at transcriptional level.


Structural and Thermodynamic bases of 14-3-3 protein interactions

14-3-3 family proteins interact with a large number of proteins that are involved in metabolism, signal transduction, apoptosis etc. We are interested in understanding the molecular recognition principles of 14-3-3 proteins interaction to their target. Our efforts are aimed at obtaining information on structural and thermodynamic features of the interaction with their targets and design small molecules that would modulate the function of protein-protein complexes.

Selected list of Publications and Patents:

  • Pandya V, Ekka MK, Dutta RK, Kumaran S (2011)
    Mass spectrometry assay for studying kinetic properties of dipeptidases: Characterization of human and yeast dipeptidases. Analytical Biochemistry 418: 134-142.

  • Kaur H, Datt M, Ekka MK, Mittal M, Singh AK, et al. (2011)
    Cys-Gly specific dipeptidase Dug1p from S. cerevisiae binds promiscuously to di-, tri-, and tetra-peptides: Peptide-protein interaction, homology modeling, and activity studies reveal a latent promiscuity in substrate recognition. Biochimie 93: 175-186.

  • Singh V, Ekka MK, Kumaran S (2012)
    Second monomer binding is the rate-limiting step in the formation of the dimeric PhoP-DNA complex. Biochemistry 51: 1346-1356.

  • Anand S, Singh V, Singh AK, Mittal M, Datt M, et al. (2012)
    Equilibrium binding and kinetic characterization of putative tetracycline repressor family transcription regulator Fad35R from Mycobacterium tuberculosis. FEBS J 279: 3214-3228.

  • Biswas D$, Pandya V$, Singh AK, Mondal AK, Kumaran S (2012)
    Co-factor binding confers substrate specificity to xylose reductase from Debaryomyces hansenii. Accepted manuscript.

  • Kumaran S et. al., (2009) J. Biol. Chem. 284 (15) 10268-75.

  • Kumaran S and Joseph M. Jez (2007) Biochemistry. 46 (18): 5586-94

  • Kumaran S*, Julie A. Francois and Joseph M. Jez (2006) Plant Cell. 18 (12): 3647-56.

  • Kumaran S, Grucza R and Waksman G (2004) Proc Natl Acad Sci U S A. 2003 100(25):14828-33.

Present group members:

  • Mary
  • Shrijita
  • Appu
  • Vijay
  • Anil (Technical Assistant-III)
This site is best viewed in Mozilla Firefox, Internet Explorer 8 and above at screen resolution of 1024 x 768 and above.