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Last Name

Deborah Perlstein, PhD

TitleAssistant Professor
InstitutionBoston University College of Arts and Sciences
DepartmentChemistry
Address590 Commonwealth Avenue
Boston MA 02215
Phone(617) 358-6180
Fax(617) 353-6466
 Research Expertise & Professional Interests
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.

 Publications
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.
List All   |   Timeline
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  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.
    View in: PubMed
  11. Bennati M, Weber A, Antonic J, Perlstein DL, Robblee J, Stubbe J. Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase. J Am Chem Soc. 2003 Dec 10; 125(49):14988-9. PMID: 14653724.
    View in: PubMed
  12. Yao R, Zhang Z, An X, Bucci B, Perlstein DL, Stubbe J, Huang M. Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways. Proc Natl Acad Sci U S A. 2003 May 27; 100(11):6628-33. PMID: 12732713.
    View in: PubMed
  13. Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. Proc Natl Acad Sci U S A. 2001 Aug 28; 98(18):10073-8. PMID: 11526233.
    View in: PubMed
  14. Ge J, Perlstein DL, Nguyen HH, Bar G, Griffin RG, Stubbe J. Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4. Proc Natl Acad Sci U S A. 2001 Aug 28; 98(18):10067-72. PMID: 11526232.
    View in: PubMed
  15. Nguyen HH, Ge J, Perlstein DL, Stubbe J. Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly. Proc Natl Acad Sci U S A. 1999 Oct 26; 96(22):12339-44. PMID: 10535923.
    View in: PubMed
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