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Faculty Profile

Michael D. Brenowitz, Ph.D.

Dr. Michael D. Brenowitz
 

Professional Interests

Biology is a dynamic process. Among the myriad array of reversible association reactions that constitute life, small molecules bind to proteins, proteins self-associate and bind to other proteins and nucleic acids and nucleic acids fold and bind to each other in elaborate processing, signaling and regulatory cascades. What is common to these processes is the physical chemistry that underlies these interactions. For example, electrostatic interactions mediate both the binding of proteins to DNA and the folding of RNA. Proteins that mimic the electrostatic character of DNA may competitively regulate DNA binding by other proteins. Our laboratory seeks answers to questions related to the structure – function relationships that govern macromolecular function by combining quantitative analysis with innovative approaches.

  • The longest running programmatic theme of our laboratory is the study of the mechanisms by which proteins recognize and bind specific sequences of DNA. We have turned our attention to proteins involved in epigenetic regulation exploring the biophysics of an epigenetic regulatory methyl-CpG binding protein MeCP2 whose disruption is causes the neurological disorder Rett Syndrome.
  • Our interest in RNA structure and folding embraces RNA aptamers, small RNA molecules selected to bind to proteins and cells with high affinity as potential diagnostic tools or therapeutics. We are studying the structure and thermodynamics of aptamer – protein complexes in order to illuminate the principals of aptamer binding and perhaps build biologically efficacious aptamers.
  • We are developing and utilizing a high-throughput method to map protein-protein interactions using amino acid side chain oxidation by the hydroxyl radical to measure solvent accessibility. The enabling techology for this project is a novel method of hydroxyl radical generation that utilizes pyrite nanocrystalline coated thermolabile plastic (‘shrinky dink’). We are using this new approach to study the structural biology of immunological complexes.
 

Selected Publications

Khrapunov, S., Warren, C., Cheng, H., Berko, E., Greally, J.M. & Brenowitz, M. (2014) Unusual characteristics of MBD, the DNA binding domain of epigenetic regulatory protein MeCP2, determine its binding specificity, Biochemistry, 53(21), 3379-91

Padlan, C.S., Malashkevich, V., Almo, S.C., Levy, M., Brenowitz, M. & Girvin, M.E. (2014) An RNA aptamer possessing a novel monovalent cation-mediated fold inhibits lysozyme catalysis by inhibiting the binding of long natural substrates, RNA, 20(4), 447-61

Schlatterer, J.C., Martin, J.S., Laederach, A.L. & Brenowitz, M. (2014) Mapping the kinetic barriers of a large RNA molecule’s folding landscape, PLoS One 9(2), e85041

Chen, C., Mitra, S., Jonikas, M., Martin, J., Brenowitz, M., Laederach, A. Biophys J. (2013) Understanding the role of 3-dimensional topology in determining the folding intermediates of group 1 introns, Biophys J. 104(6), 1326-37

Schlatterer, J.C., Wieder, M.S., Jones, C.D., Pollack, L. & Brenowitz, M. (2012) Pyrite footprinting of RNA, Biochem Biophys Res Commun.,  425(2), 374 - 378

 

Material in this section is provided by individual faculty members who are solely responsible for its accuracy and content.

Contact

Albert Einstein College of Medicine
Jack and Pearl Resnick Campus
1300 Morris Park Avenue
Forchheimer Building, Room 311
Bronx, NY 10461

Tel: 718.430.3179
michael.brenowitz@einstein.yu.edu

 
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