Welcome to the Patel Lab
Department of Biochemistry and Molecular Biology
Rutgers - Robert Wood Johnson Medical School
The overarching goal of our research is to understand the molecular mechanisms of enzymes in DNA replication, DNA transcription, and pathogen recognition.
Our current research investigates the structure and mechanisms of (i) RNA polymerases and transcription factors that catalyze mitochondrial DNA transcription, (ii) replicative DNA helicase-primase and polymerases that catalyze phage T7 and mitochondrial DNA replication, and (ii) RIG-I and LGP2 innate immune receptors that detect common viruses.
We strive to quantitatively characterize the elementary steps of the enzymatic reactions, including motor proteins that drive DNA replication, transcription, and viral RNA recognition by the RIG-I like innate immune receptors. This is achieved through a multidisciplinary approach that employs a combination of structural, biochemical, biophysical, and computational modeling methods and studies the transient state and single molecule kinetics of enzyme reactions. Our research has application in biotechnology and therapeutics.
News
NIGMS MIRA grant
Lab receives an NIH MIRA grant to study the mechanisms of enzymes involved in DNA replication, transcription, and innate immunity.
Transcriptional fidelities of mitochondrial and T7 RNA polymerases. Sultana S et al. J. Biol. Chem. 2017
This work measures the base substitution error rates of three single-subunit RNA polymerases from T7, yeast and human mitochondria. Although the base substitution error rates are one in a million or tenth of a million, the mutagenic bypass rates are high and in the human mitochondrial RNA polymerase this is exacerbated by the transcription factor, TEFM.
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TFB2M and TFAM synergistically melt the human mitochondrial DNA promoter. Ramachandran A et al. Nucleic Acids Res. 2016
This work provides a basic characterization of the DNA structure in the initiation complex of the human mitochondrial RNA polymerase, and shows that the promoter DNA is melted from -4 to +2, and both transcription factors, TFB2M and TFAM, are required for promoter opening.
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Self and non-self RNA recognition by the RIG-I. Devarkar et al. Proc. Natl. Acad. Sci. USA 2016
This work shows that self RNAs evade RIG-I recognition by 2'-O-methylation of the 5'-end ribose, and 7mG capping itself is not sufficient. RIG-I uses H830 as a sensor to avoid activation by self RNAs. Structures and biochemical analyses provide insights into the mechanisms of host and viral immune evasion from RIG-I.
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T7 DNA helicase and polymerase are juxtaposed close to the fork junction during leading strand synthesis. Nandakumar et al. ELife 2015
This work shows that the replicative T7 DNA helicase and DNA polymerase enzymes perform their functions juxtaposed close to the leading strand fork junction. The work provides evidence on how the two motor proteins synergistically melt the double stranded DNA at the fork junction.
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SWAPNIL D. WINS SHATKIN AWARD
Swapnil Devarkar was awarded the Aaron Shatkin Graduate Scholarship by The Graduate School of Biomedical Sciences - New Brunswick/Piscataway Division. Dr. Aaron Shatkin was the founding director of the Center for Advanced Biotechnology and Medicine.
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Urmimala B. awarded AHA fellowship
Urmimala Basu was awarded the American Heart Association Predoctoral Fellowship to study the mechanism of human mitochondrial transcription enzymes.
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