Pushpalatha Murthy

Pushpalatha Murthy

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Professor, Chemistry

  • Postdoctoral Fellow, University of Michigan, Ann Arbor, Michigan
  • PhD, Brown University, Providence, Rhode Island
  • MSc, Indian Institute of Technology, Kanpur, India
  • BSc, Delhi University, New Delhi, India

Biography

It is well-established that in animal cells phosphoinositides play a central role in signal transduction by undergoing signal-stimulated hydrolysis to generate second messengers. However, the biochemical aspects of phosphoinositides in plant cells is not well-understood. Dr. Murthy's research group is investigating the structure, metabolism and biological role of phosphoinositides in plant cells. In their effort to characterize the structure of phosphoinositides in barley seeds, they discovered the presence of novel scyllo-inositol containing phosphoinositides. Currently, they are investigating the biosynthesis, subcellular localization, and biological role of this novel class of phosphoinositides. In addition, the involvement of phosphoinositides in gibberellin-triggered alpha-amylase synthesis is being investigated. A variety of purification techniques such as chromatography, high-voltage paper electrophoresis, HLPC, and spectroscopic techniques such as NMR, 2D NMR, IR, and GC-MS is employed in this project.

The second messenger role of inositol-1,4,5-triphosphate has generated a great deal of interest in the structure and metabolism of inositol phosphates. Phytic acid, myo-inositol hexakis phosphate, is the major storage form of inositol phosphates. Recent work has established the presence of phytic acid in a variety of micro-organisms and animal cells. Phytases are the primary enzymes responsible for the degradation of phytic acid. Dr. Murthy's research group is investigating various catalytic and structural aspects of phytases including; specificity of hydrolysis, molecular weight and subunit structure, amino acid sequence and molecular biology.

Research Interests

  • Structure, metabolism, and biological role of phosphoinositides in plant cells
  • Catalytic and structural aspects of phytases, including specificity of hydrolysis, molecular weight and subunit structure, amino acid sequence, and molecular biology
  • Biosynthesis, subcellular localization, and biological role of novel scyllo-inositol containing phosphoinositides

Recent Publications

  • S.C. Johnson, M.Yang, P.P.N. Murthy (2010) Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris. Protein Express. Purif. 74, 196-203.
  • C. Xue, S. Velayudhan, S. C. Johnson, R. Saha, A. Smith#, W. Brewer, P.P.N. Murthy, ST. Bagley, Haiying Liu (2009) Highly water –soluble, fluorescent, conjugated fluorine-based glycopolymers with poly(ethylene glycol)-tethereed spacers for sensitive detection of Escherichia coli. Chem. Eur. J. 15, 2289-2295.
  • Pushpalatha P.N. Murthy (2007) Identification of inositol phosphates by NMR spectroscopy: unraveling structural diversity. In Proceedings of the Bouyoucos conference on Biogeochemical interaction of inositol phosphates in the environment, B.L. Turner, A.E. Richardson, and E.J. Mullaney (Editors), CB international, Cambridge, MA, pp 7-22
  • Ping Yang, Bernard Spiess, Pushpalatha P.N. Murthy, Richard E. Brown (2007) Influence of metal cations on the intramolecular hydrogen-bonding network in phosphorylated compounds. J. Phys. Chem. 111, 3602-3612
  • Cuihua Xue, Sonali P. Jog, Pushpalatha P. N. Murthy, and Haiying Liu (2006) Synthesis of highly water-soluble fluorescent conjugated glycopoly(p-phenylene)s for lectin and Escherichia coli. Biomacromolecules, 7, 2470-2474
  • Bakul Dhagat Mehta, Sonali P. Jog, Steven C. Johnson and Pushpalatha P.N. Murthy (2006) Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphopsphate phosphatase (MINPP), Phytochemistry, 67, 1874-1886.
  • B.G. Garchow, S.P. Jog, B. D. Mehta, J.M. Monosso (posthumous), P.P.N. Murthy (2006) Alkaline phytase from Lilium longiflorum: purification and structural characterization. Protein Express. Purif. 46, 221-232.