Satish K Nair

About

Satish K Nair is a professor in the Department of Biochemistry at the University of Illinois, with additional affiliations including the Center for Biophysics and Quantitative Biology, the School of Molecular and Cellular Biology, the Materials Research Lab, and the Carl R. Woese Institute for Genomic Biology. His research focuses on understanding the biosynthesis and application of bacterial natural products through biochemical, microbiological, and biophysical techniques, particularly X-ray crystallography. His work includes studying how bacteria produce small molecules that regulate intra-species behavior or combat competing species, with implications for developing therapeutic agents against pathogens. Nair's research encompasses the biosynthesis of ribosomally synthesized peptide antibiotics such as lantibiotics and cyanobactins, as well as phosphonate biosynthesis and engineering. He investigates bacterial inter- and intracellular communication mechanisms, including quorum sensing and diffusible signal factors, aiming to identify targets for therapeutic intervention. His educational background includes a B.S. from Brown University, a Ph.D. from the University of Pennsylvania, and postdoctoral work at Rockefeller University. His contributions advance understanding of natural product biosynthesis, enzyme mechanisms, and bacterial signaling pathways.

Research topics

• Biology
• Computer Science
• Computational biology
• Biochemistry
• Data science
• Engineering
• Bioinformatics
• Genetics
• Combinatorial chemistry
• Chemistry

Selected publications

• New developments in RiPP discovery, enzymology and engineering

  Natural Product Reports · 2020 · 780 citations

  Covering: up to June 2020Ribosomally-synthesized and post-translationally modified peptides (RiPPs) are a large group of natural products. A community-driven review in 2013 described the emerging commonalities in the biosynthesis of RiPPs and the opportunities they offered for bioengineering and genome mining. Since then, the field has seen tremendous advances in understanding of the mechanisms by which nature assembles these compounds, in engineering their biosynthetic machinery for a wide rang…

  DOI

• Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides

  Chemical Reviews · 2022 · 159 citations

  Senior authorCorresponding

  Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a natural product class that has undergone significant expansion due to the rapid growth in genome sequencing data and recognition that they are made by biosynthetic pathways that share many characteristic features. Their mode of actions cover a wide range of biological processes and include binding to membranes, receptors, enzymes, lipids, RNA, and metals as well as use as cofactors and signaling molecules. This revi…

  DOI

• LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome

  Cell · 2021 · 55 citations

  Enzyme-mediated damage repair or mitigation, while common for nucleic acids, is rare for proteins. Examples of protein damage are elimination of phosphorylated Ser/Thr to dehydroalanine/dehydrobutyrine (Dha/Dhb) in pathogenesis and aging. Bacterial LanC enzymes use Dha/Dhb to form carbon-sulfur linkages in antimicrobial peptides, but the functions of eukaryotic LanC-like (LanCL) counterparts are unknown. We show that LanCLs catalyze the addition of glutathione to Dha/Dhb in proteins, driving irr…

  DOI

• A biocatalytic platform for asymmetric alkylation of α-keto acids by mining and engineering of methyltransferases

  Nature Communications · 2023-09-14 · 29 citations

  articleOpen access

  Abstract Catalytic asymmetric α-alkylation of carbonyl compounds represents a long-standing challenge in synthetic organic chemistry. Herein, we advance a dual biocatalytic platform for the efficient asymmetric alkylation of α-keto acids. First, guided by our recently obtained crystal structures, we develop SgvM VAV as a general biocatalyst for the enantioselective methylation, ethylation, allylation and propargylation of a range of α-keto acids with total turnover numbers (TTNs) up to 4,600. Se…

  PublisherOA PDFDOI

• Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin

  Nature Communications · 2024-06-18 · 24 citations

  articleOpen access

  The receptor-binding site of influenza A virus hemagglutinin partially overlaps with major antigenic sites and constantly evolves. In this study, we observe that mutations G186D and D190N in the hemagglutinin receptor-binding site have coevolved in two recent human H3N2 clades. X-ray crystallography results show that these mutations coordinately drive the evolution of the hemagglutinin receptor binding mode. Epistasis between G186D and D190N is further demonstrated by glycan binding and thermost…

  PublisherOA PDFDOI

Recent grants

• Structural Biological Studies of Thipeptide Biosynthesis and Engineering

  NIH · $1.2M · 2019–2024

• Exploring Peptide Conjugates as Trojan Horse Systems for Drug Design and Discovery

  NIH · $2.2M · 2015–2020

• NIH Grant R56AI117210

  NIH · $467k · 2015

Frequent coauthors

• Wilfred A. van der Donk

  Howard Hughes Medical Institute

  89 shared

• Vinayak Agarwal

  IIT@MIT

  48 shared

• Konstantin Severinov

  Rutgers, The State University of New Jersey

  46 shared

• Isaac Cann

  University of Illinois Urbana-Champaign

  30 shared

• Jonathan R. Chekan

  University of North Carolina at Greensboro

  28 shared

• Douglas A. Mitchell

  Vanderbilt University

  28 shared

• Roderick I. Mackie

  University of Illinois Urbana-Champaign

  25 shared

• D.W. Christianson

  California University of Pennsylvania

  25 shared

Labs

• Center for Biophysics and Quantitative BiologyPI

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