Cooper Medical School of Rowan University
Department of Biomedical Sciences
401 South Broadway
Camden, NJ 08103
University of Poona, Pune, India
Cold shock, RNA chaperones, Toxin-antitoxin;active learning, medical education
I have been pursuing research on cold shock response and adaptation of bacteriawith special emphasis on RNA chaperone function of cold shock proteins. Weshowed that the transcription antitermination activity of the CspA homologuesis essential for their critical function in cold acclimation of cells and thisactivity depends on their nucleic acid melting activity. These observations in Escherichiacoli hold true for diverse organismssuch as thermophilic bacteria and were used as guidelines and found to be truein higher systems such as plants by other research groups. We elucidated the mechanismsunderlying the RNA chaperone function of Csps. Using detail DNA microarrayanalysis of cold shock response of E.coli cells and its cold-sensitivemutants, we discovered cellular targets of CspA homologues and other cold shockproteins such as IF1. A new class of rho-independent,Csp-responsive transcription terminators emerged from bioinformatics analysisof these data which shed more light on the cold-acclimation-essential RNAchaperone function of CspA homologues. We have developed biotechnologicalapplications using various novel properties of Csps, for example, cold-shockvectors for protein production at low temperatures. I am also working onelucidating the role of cold shock proteins such as CsdA, PNPase and RNase R inRNA metabolism at low temperature and have now started to work on the bacterialtoxin-antitoxin systems. We recently characterized one such E. colitoxin LdrA and showed that another E.colitoxin, MazF has antitumor activity.
Yamaguchi Y,Tokunaga N, Inouye M and Phadtare S. Characterization of LdrAprotein of Escherichia coli. Journalof Molecular Microbiology and Biotechnology. 2014; 24:91-97.
Phadtare S. Escherichia coli cold-shock geneprofiles in response to overexpression/deletion of CsdA, RNase R and PNPase andrelevance to low-temperature RNA metabolism. Genes to Cells. 2012; 17:850-74.
Phadtare S. Unwinding activity of cold shock proteins and RNAmetabolism. RNA Biology. 2011; 8:394-734.
Awano N, Rajagopal V, Arbing M, Patel S, Hunt J, Inouye M and Phadtare S. Escherichia coliRNase R has dual activities, helicase and ribonuclease. Journal of Bacteriology.2010; 192:1344-52.
Awano N, Inouye M and Phadtare S. RNase activity of polynucleotide phosphorylase is critical at lowtemperature in Escherichia coli andis complemented by RNase II. Journal of Bacteriology. 2008; 190:5924-33.
Awano N, Xu C, Ke H, Inoue K, Inouye M and PhadtareS. Complementation analysis of the cold-sensitive phenotype of the Escherichia coli csdA deletion strain. Journalof Bacteriology. 2007; 189: 5808-15.
Phadtare S and Severinov K. Nucleic acid meltingby Escherichia coli CspE. NucleicAcids Research. 2005; 33:5583-5590.
Inouye M and PhadtareS. Cold-shock response and adaptation at near-freezing temperature in micro-organisms.Science STKE. 2004; 237:(pe26).
Phadtare S, Tyagi S, Inouye M andSeverinov K. Three amino acids in Escherichiacoli CspE surface-exposed aromatic patch are critical for nucleic acidmelting activity leading to transcription antitermination and cold acclimationof cells. Journal of Biological Chemistry. 2002; 277:46706-46711.
Phadtare S, Inouye M and Severinov K.The nucleic acid melting activity of Escherichiacoli CspE is critical for transcription antitermination andcold-acclimation of cells. Journal of Biological Chemistry. 2002;277:7239-7245.
Phadtare S, Abali E andBrodsky B. Over The Counter Drugs (and food supplement) exercise: A team basedintroduction to biochemistry for health professional students. Biochemistry andMolecular Biology Education. 2013; 41:384-387.
Phadtare S, Galt J and BrodskyB. Active learning approaches for nutrition education in the medical schoolcurriculum. Medical Science Educator. 2014; 24: 27-33.
Abali E, Phadtare S,Galt J and Brodsky B. An online, guided e-journal exercise. Biochemistry andMolecular Biology Education. 2014; 42:259-69.