Deborah Perlstein, PhD
Assistant Professor
Boston University College of Arts and Sciences
Dept of Chemistry

PhD, Massachusetts Institute of Technology



Deborah Perlstein joined the Department of Chemistry in July 2010. While new to Boston University, she has called Boston her home since arriving in the fall of 1998 to pursue her Ph.D. at MIT. More recently, she was an NIH Postdoctoral Fellow in the laboratory of Suzanne Walker in the Department of Microbiology and Molecular Genetics at Harvard Medical School.

The research the Perlstein Group lies at the interface of chemistry and biology with a focus on bioinorganic chemistry. We are currently developing new projects that will use the tools of chemical biology, including biophysical techniques, enzymology, microscopy, and molecular biology to understand iron-sulfur cluster containing proteins and bacterial cell division.

Iron-sulfur proteins: Iron-sulfur clusters are ancient and essential cofactors that allow proteins to access a wide range of chemistries that would not otherwise be possible with the standard 20 amino acids. Elucidating the novel chemical mechanisms of enzymes that utilize iron-sulfur clusters and understanding the biochemical pathway required for iron sulfur cluster assembly in vivo will be a major focus of the lab’s research efforts.

Bacterial Cell Division: The bacterial cytoskeletal proteins MreB and FtsZ are the major orchestrators of cell growth and division and therefore represent potential antibiotic targets that can be exploited to combat drug resistant pathogens. These bacterial homologs of actin and tubulin coordinate the activities of numerous enzymes in the cell membrane and the perplasmic space that maintain the integrity of the bacterial cell envelope during growth and division. We are developing projects to probe how cytoskeletal protein dynamics are regulated both in vitro and in vivo to discover new approaches to combating drug resistant microorganisms.


CAREER: Elucidating the role of ATP in Cytosolic Iron Sulfur Cluster Biogenesis
05/01/2016 - 04/30/2021 (PI)
National Science Foundation
CHE-1555295




Yr Title Project-Sub Proj Pubs
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.

  1. Camire EJ, Grossman JD, Thole GJ, Fleischman NM, Perlstein DL. The Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPase. J Biol Chem. 2015 Sep 25; 290(39):23793-802. PMID: 26195633; PMCID: PMC4583046; DOI: 10.1074/jbc.M115.667022;.
  2. Doud EH, Perlstein DL, Wolpert M, Cane DE, Walker S. Two distinct mechanisms for TIM barrel prenyltransferases in bacteria. J Am Chem Soc. 2011 Feb 9; 133(5):1270-3. PMID: 21214173; PMCID: PMC3033458; DOI: 10.1021/ja109578b;.
  3. Perlstein DL, Wang TS, Doud EH, Kahne D, Walker S. The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases. J Am Chem Soc. 2010 Jan 13; 132(1):48-9. PMID: 20017480; PMCID: PMC2830065; DOI: 10.1021/ja909325m;.
  4. Lupoli TJ, Taniguchi T, Wang TS, Perlstein DL, Walker S, Kahne DE. Studying a cell division amidase using defined peptidoglycan substrates. J Am Chem Soc. 2009 Dec 30; 131(51):18230-1. PMID: 19957935; PMCID: PMC2871763; DOI: 10.1021/ja908916z;.
  5. Ostash B, Doud EH, Lin C, Ostash I, Perlstein DL, Fuse S, Wolpert M, Kahne D, Walker S. Complete characterization of the seventeen step moenomycin biosynthetic pathway. Biochemistry. 2009 Sep 22; 48(37):8830-41. PMID: 19640006; PMCID: PMC2747051; DOI: 10.1021/bi901018q;.
  6. Perlstein DL, Zhang Y, Wang TS, Kahne DE, Walker S. The direction of glycan chain elongation by peptidoglycan glycosyltransferases. J Am Chem Soc. 2007 Oct 24; 129(42):12674-5. PMID: 17914829; PMCID: PMC3206585.
  7. Ortigosa AD, Hristova D, Perlstein DL, Zhang Z, Huang M, Stubbe J. Determination of the in vivo stoichiometry of tyrosyl radical per betabeta'' in Saccharomyces cerevisiae ribonucleotide reductase. Biochemistry. 2006 Oct 10; 45(40):12282-94. PMID: 17014081; PMCID: PMC4674157.
  8. Zhang Z, An X, Yang K, Perlstein DL, Hicks L, Kelleher N, Stubbe J, Huang M. Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein. Proc Natl Acad Sci U S A. 2006 Jan 31; 103(5):1422-7. PMID: 16432237; PMCID: PMC1360584.
  9. Perlstein DL, Ge J, Ortigosa AD, Robblee JH, Zhang Z, Huang M, Stubbe J. The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo. Biochemistry. 2005 Nov 22; 44(46):15366-77. PMID: 16285741; PMCID: PMC4669231.
  10. Sommerhalter M, Voegtli WC, Perlstein DL, Ge J, Stubbe J, Rosenzweig AC. Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers. Biochemistry. 2004 Jun 22; 43(24):7736-42. PMID: 15196016.
Showing 10 of 15 results. Show More

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 15 publications over 11 distinct years, with a maximum of 2 publications in 2001 and 2003 and 2006 and 2009

YearPublications
19991
20012
20032
20041
20051
20062
20071
20092
20101
20111
20151
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