
Deborah Perlstein
· Associate Professor, Director of Undergraduate StudiesBoston University · Chemistry
Active 1947–2026
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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…
Biochemistry · 2019-03-13 · 20 citations
articleSenior authorCorrespondingThe 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…
Biochemistry · 2017-05-25 · 19 citations
articleSenior authorCorrespondingThe 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 authorThe 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…
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
CAREER: Elucidating the role of ATP in Cytosolic Iron Sulfur Cluster Biogenesis
NSF · $778k · 2016–2022
The mechanism of apo-target recognition in cytsolic iron sulfur cluster biosynthesis
NIH · $1.6M · 2018–2024
NIH · $96k · 2009
Frequent coauthors
- 37 shared
JoAnne Stubbe
- 28 shared
Mingxia Huang
Shenyang Jianzhu University
- 19 shared
Jie Ge
Air Force Medical University
- 18 shared
Allison D. Ortigosa
Merck & Co., Inc., Rahway, NJ, USA (United States)
- 13 shared
John H. Robblee
Momenta Pharmaceuticals (United States)
- 10 shared
Zhen Zhang
China Medical University
- 10 shared
Xiuxiang An
Jinzhou Medical University
- 9 shared
Zhen Zhang
Hunan University
Labs
Perlstein GroupPI
Education
- 2005
Ph.D., Chemistry
Massachusetts Institute of Technology
- 1998
BA
Tulane University
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