Research Groups

Molecular Medicine: Membrane Protein Biology

Research Interests and Description

Group Leader: Arockiasamy Arulandu, PhD

Research Interests

Structural Biology, Membrane Proteins, P-type ATPases, Type VII Secretion System (T7SS), Eukaryotic Ion-Channels

Description of Research

Structural Biology of Mycobacterial membrane proteins
Membrane proteins, coded by genes comprising 20 to 30% of a given genome, carry out vital biological processes such us ion transport, energy generation, signal transduction and protein secretion. However, molecular understanding of their biological function is very minimal due to lack of adequate structure-function information. The research focus is to uncover the molecular mechanisms underlining few such processes; metal-ion transport and virulent protein translocation in Mycobacteria, in particular Mycobacterium tuberculosis (M. tb). Genome of M. tb codes for several P-type ATPase metal-ion transporters, of which some are essential for virulence. Hence, a systematic approach is undertaken to characterize metal-ion selection, delivery, and transport by these putative transporters. Three type VII Secretion System (T7SS) machinery are functional in M. tb (ESX-1 and ESX-3 and ESX-5) and are essential for growth in vitro and in vivo. To define substrate protein secretion mechanisms, we are attempting to reconstitute minimal functional T7SS protein secretion complex. In addition,we work on novel ion-channels from higher eukaryotes, which are linked to several cancers. We use biochemical and structural molecular biological tools to help achieve our goals.


Maindola, P., Raina, R., Goyal, P., Atmakuri, K., Ojha, A., Gupta, S., Christie, P.J., Iyer, L.M., Aravind, L., Arockiasamy, A. 2014. Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids. Nature Comm 5, Art. no. 5322 doi:10.1038/ncomms6322 

Balasubramaniam, D., Arockiasamy, A., Kumar, P. D., Sharma, A., Krishnaswamy, S. 2012. Asymmetric pore occupancy in crystal structure of OmpF porin from Salmonella typhi. J Struct Biol 178, 233-244 PubMed link

Kashyap, M., Jagga, Z., Das, B.K., Arockiasamy, A., Bhavesh, N.S. 2011. 1H, 13C and 15N NMR assignments of inactive form of P1 endolysin Lyz. Biomol NMR Assign In press PubMed link

Arockiasamy, A., Aggarwal, A., Savva, C.G., Holzenburg, A., Sacchettini, J.C. 2011. Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site. Protein Sci 5, 827-833 PubMed link

Sun, Q., Kuty, G.F., Arockiasamy, A., Xu, M., Young, R., Sacchettini, J.C. 2009. Regulation of a muralytic enzyme by dynamic membrane topology. Nat Struct Mol Biol 11, 1192-1194 PubMed link

Xu, M., Arulandu, A., Struck, D.K., Swanson, S., Sacchettini, J.C., Young, R. 2005. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307, 113-117 PubMed link

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