Deborah Perlstein | Profiles RNS

Deborah Perlstein, PhD

Associate Professor

Boston University College of Arts and Sciences

Chemistry

PhD, Massachusetts Institute of Technology
BS, Tulane University

Websites

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ORCID : 0000-0002-7124-9896

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.

Member
Boston University
Evans Center for Interdisciplinary Biomedical Research

BU Research

The mechanism of apo-target recognition in cytosolic iron sulfur cluster biosynthesis
09/05/2018 - 06/30/2024 (PI)
NIH/National Institute of General Medical Sciences
5R01GM121673-05

CAREER: Elucidating the role of ATP in Cytosolic Iron Sulfur Cluster Biogenesis
05/01/2016 - 04/30/2022 (PI)
National Science Foundation
CHE-1555295

Title

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.

iCite Analysis Copy PMIDs To Clipboard

Vasquez S, Marquez MD, Brignole EJ, Vo A, Kong S, Park C, Perlstein DL, Drennan CL. Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway. Commun Biol. 2023 Dec 18; 6(1):1276. PMID: 38110506; PMCID: PMC10728100; DOI: 10.1038/s42003-023-05579-3;

Marquez MD, Greth C, Buzuk A, Liu Y, Blinn CM, Beller S, Leiskau L, Hushka A, Wu K, Nur K, Netz DJA, Perlstein DL, Pierik AJ. Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide. Proc Natl Acad Sci U S A. 2023 Oct 31; 120(44):e2311057120. PMID: 37883440; PMCID: PMC10623007; DOI: 10.1073/pnas.2311057120;

Marquez MD, Greth C, Buzuk A, Liu Y, Blinn CM, Beller S, Leiskau L, Hushka A, Wu K, Nur K, Netz DJ, Perlstein DL, Pierik AJ. Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide. bioRxiv. 2023 May 20. PMID: 37292740; PMCID: PMC10245660; DOI: 10.1101/2023.05.19.541488;

Molé CN, Dave K, Perlstein DL. Methods to Unravel the Roles of ATPases in Fe-S Cluster Biosynthesis. Methods Mol Biol. 2021; 2353:155-171. PMID: 34292549

Grossman JD, Gay KA, Camire EJ, Walden WE, Perlstein DL. Coupling Nucleotide Binding and Hydrolysis to Iron-Sulfur Cluster Acquisition and Transfer Revealed through Genetic Dissection of the Nbp35 ATPase Site. Biochemistry. 2019 04 16; 58(15):2017-2027. PMID: 30865432

Grossman JD, Camire EJ, Glynn CA, Neil CM, Seguinot BO, Perlstein DL. The Cfd1 Subunit of the Nbp35-Cfd1 Iron Sulfur Cluster Scaffolding Complex Controls Nucleotide Binding. Biochemistry. 2019 03 26; 58(12):1587-1595. PMID: 30785732

Vo A, Fleischman NM, Froehlich MJ, Lee CY, Cosman JA, Glynn CA, Hassan ZO, Perlstein DL. Identifying the Protein Interactions of the Cytosolic Iron-Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets. Biochemistry. 2018 04 24; 57(16):2349-2358. PMID: 28539047

Grossman JD, Camire EJ, Perlstein DL. Approaches to Interrogate the Role of Nucleotide Hydrolysis by Metal Trafficking NTPases: The Nbp35-Cfd1 Iron-Sulfur Cluster Scaffold as a Case Study. Methods Enzymol. 2018; 599:293-325. PMID: 29746244

Vo AT, Fleischman NM, Marquez MD, Camire EJ, Esonwune SU, Grossman JD, Gay KA, Cosman JA, Perlstein DL. Defining the domains of Cia2 required for its essential function in vivo and in vitro. Metallomics. 2017 Nov 15; 9(11):1645-1654. PMID: 29057997

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;

Showing 10 of 24 results. Show More

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;

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;

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;

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;

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; DOI: 10.1021/ja075965y;

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; DOI: 10.1021/bi0610404;

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; DOI: 10.1073/pnas.0510516103;

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; DOI: 10.1021/bi051616+;

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

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

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; PMCID: PMC164498

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; PMCID: PMC56916

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; PMCID: PMC56917

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; PMCID: PMC22918

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

Bar chart showing 24 publications over 16 distinct years, with a maximum of 3 publications in 2023

Bar chart showing 24 publications over 16 distinct years, with a maximum of 3 publications in 2023

Year	Publications
1999	1
2001	2
2003	2
2004	1
2005	1
2006	2
2007	1
2009	2
2010	1
2011	1
2015	1
2017	1
2018	2
2019	2
2021	1
2023	3

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