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Deborah Perlstein

Deborah Perlstein

· Associate Professor, Director of Undergraduate Studies

Boston University · Chemistry

Active 1947–2026

h-index24
Citations1.2k
Papers478 last 5y
Funding$2.5M

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Deborah Perlstein is an Associate Professor and the Director of Undergraduate Studies in the Department of Chemistry at Boston University. Her research lies at the interface of chemistry and biology, with a focus on bioinorganic chemistry. Her group is developing projects that utilize chemical biology tools, including biophysical techniques, enzymology, microscopy, and molecular biology, to understand iron-sulfur cluster containing proteins and bacterial cell division. She has demonstrated the use of site-specific substrate analogs to reveal distinct lipid lengths for donor and acceptor sites in peptidoglycan glycosyltransferases. Her work on iron-sulfur proteins involves elucidating the chemical mechanisms of enzymes that utilize iron-sulfur clusters and understanding the biochemical pathways for iron-sulfur cluster assembly in vivo. Additionally, her research on bacterial cell division investigates the roles of cytoskeletal proteins MreB and FtsZ, which are key to bacterial growth and division, and explores their regulation both in vitro and in vivo to identify new approaches to combat drug-resistant pathogens. Dr. Perlstein earned her B.S. in Biological Chemistry from Tulane University in 1998, her Ph.D. in Biochemistry from MIT in 2005, and completed a postdoctoral fellowship in Microbiology and Chemical Biology at Harvard Medical School in 2010. She has mentored numerous undergraduate students, graduate students, and postdoctoral researchers, with notable collaborations…

Research topics

  • Computer Science
  • Cell biology
  • Biology
  • Biochemistry
  • Chemistry
  • Organic chemistry
  • Biophysics
  • Computational biology
  • Computer network

Selected publications

  • Cytosolic iron–sulfur protein assembly system identifies clients by a C-terminal tripeptide

    Proceedings of the National Academy of Sciences · 2023 · 23 citations

    tripeptide is present at the C-terminus of more than a quarter of clients or their adaptors. When present, this targeting complex recognition (TCR) motif is necessary and sufficient for binding to the CTC in vitro and for directing Fe-S cluster delivery in vivo. Remarkably, fusion of this TCR signal enables engineering of cluster maturation on a nonnative protein via recruitment of the CIA machinery. Our study advances our understanding of Fe-S protein maturation and paves the way for bioenginee…

  • Coupling Nucleotide Binding and Hydrolysis to Iron–Sulfur Cluster Acquisition and Transfer Revealed through Genetic Dissection of the Nbp35 ATPase Site

    Biochemistry · 2019-03-13 · 20 citations

    articleSenior authorCorresponding

    The cytosolic iron-sulfur cluster assembly (CIA) scaffold, comprising Nbp35 and Cfd1 in yeast, assembles iron-sulfur (FeS) clusters destined for cytosolic and nuclear enzymes. ATP hydrolysis by the CIA scaffold plays an essential but poorly understood role in cluster biogenesis. Here we find that mutation of conserved residues in the four motifs comprising the ATPase site of Nbp35 diminished the scaffold's ability to both assemble and transfer its FeS cluster in vivo. The mutants fall into four…

  • Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets

    Biochemistry · 2017-05-25 · 19 citations

    articleSenior authorCorresponding

    The cytosolic iron-sulfur cluster assembly (CIA) system assembles iron-sulfur (FeS) cluster cofactors and inserts them into >20 apoprotein targets residing in the cytosol and nucleus. Three CIA proteins, called Cia1, Cia2, and Met18 in yeast, form the targeting complex responsible for apo-target recognition. There is little information about the structure of this complex or its mechanism of CIA substrate recognition. Herein, we exploit affinity co-purification and size exclusion chromatography t…

  • Defining the domains of Cia2 required for its essential function <i>in vivo</i> and <i>in vitro</i>

    Metallomics · 2017-01-01 · 12 citations

    articleSenior author

    The cytosolic iron-sulfur cluster assembly (CIA) system biosynthesizes iron-sulfur (FeS) cluster cofactors for cytosolic and nuclear proteins. The yeast Cia2 protein is the central component of the targeting complex which identifies apo-protein targets in the final step of the pathway. Herein, we determine that Cia2 contains five conserved motifs distributed between an intrinsically disordered N-terminal domain and a C-terminal domain of unknown function 59 (DUF59). The disordered domain is disp…

  • Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway

    Communications Biology · 2023 · 7 citations

    Iron-sulfur clusters are essential for life and defects in their biosynthesis lead to human diseases. The mechanism of cluster assembly and delivery to cytosolic and nuclear client proteins via the cytosolic iron-sulfur cluster assembly (CIA) pathway is not well understood. Here we report cryo-EM structures of the HEAT-repeat protein Met18 from Saccharomyces cerevisiae, a key component of the CIA targeting complex (CTC) that identifies cytosolic and nuclear client proteins and delivers a mature…

Recent grants

Frequent coauthors

  • JoAnne Stubbe

    37 shared
  • Mingxia Huang

    Shenyang Jianzhu University

    28 shared
  • Jie Ge

    Air Force Medical University

    19 shared
  • Allison D. Ortigosa

    Merck & Co., Inc., Rahway, NJ, USA (United States)

    18 shared
  • John H. Robblee

    Momenta Pharmaceuticals (United States)

    13 shared
  • Zhen Zhang

    China Medical University

    10 shared
  • Xiuxiang An

    Jinzhou Medical University

    10 shared
  • Zhen Zhang

    Hunan University

    9 shared

Labs

  • Perlstein GroupPI

Education

  • Ph.D., Chemistry

    Massachusetts Institute of Technology

    2005
  • BA

    Tulane University

    1998

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