About

Robert Landick is a Professor of Biochemistry at the University of Wisconsin-Madison, within the Department of Bacteriology. He is based in the Microbial Sciences Building located at 1550 Linden Dr., Madison, WI 53706. As a faculty member, he is involved in research and teaching activities related to biochemistry and microbiology. His contact information includes a phone number (608) 265-8475 and an email address landick@bact.wisc.edu. Further details about his research focus, background, and key contributions are not provided on the page.

Research topics

• Biology
• Genetics
• Cell biology
• Computer Science
• Molecular biology
• Biochemistry
• Computational biology
• Chemistry
• Virology

Selected publications

• ppGpp regulates transcription elongation via direct and indirect inputs to RNA polymerase pausing and nucleotide addition

  Zenodo (CERN European Organization for Nuclear Research) · 2027-04-03

  articleOpen access1st authorCorresponding

  The signaling molecules guanosine 5′-tri/diphosphate 3′-diphosphate, (p)ppGpp, control bacterial protein synthesis rates and cell growth by targeting transcription, translation, NTP synthesis, and other functions. In lineages like E. coli, (p)ppGpp produced in response to charged-tRNA deficiency targets transcribing RNAP polymerase (RNAP) to match its pace to the pioneering ribosome on the nascent RNA (transcription–translation coupling). However, the mechanism by which (p)ppGpp slows RNAP is poorly defined. (p)ppGpp may allosterically stimulate RNAP pausing, inhibit catalysis, promote backtracking, compete for substrate GTP, inhibit GTP synthesis, or uncouple transcription–translation by inhibiting translation. Using a combination of cryo-EM, biochemical assays, and quantitative nascent elongating transcript sequencing (qNET-seq), we establish that (p)ppGpp allosterically regulates pausing and nucleotide addition via distinct motions of the RNAP swivel module and both competes with and lowers GTP in vivo. (p)ppGpp stimulates swiveling at pause sites to delay escape but may also inhibit counter-swiveling required in every round of nucleotide addition. This repository stores the custom code accompanying this manuscript.

  PublisherDOI

• ppGpp regulates transcription elongation via direct and indirect inputs to RNA polymerase pausing and nucleotide addition

  Zenodo (CERN European Organization for Nuclear Research) · 2027-04-03

  articleOpen access1st authorCorresponding

  The signaling molecules guanosine 5′-tri/diphosphate 3′-diphosphate, (p)ppGpp, control bacterial protein synthesis rates and cell growth by targeting transcription, translation, NTP synthesis, and other functions. In lineages like E. coli, (p)ppGpp produced in response to charged-tRNA deficiency targets transcribing RNAP polymerase (RNAP) to match its pace to the pioneering ribosome on the nascent RNA (transcription–translation coupling). However, the mechanism by which (p)ppGpp slows RNAP is poorly defined. (p)ppGpp may allosterically stimulate RNAP pausing, inhibit catalysis, promote backtracking, compete for substrate GTP, inhibit GTP synthesis, or uncouple transcription–translation by inhibiting translation. Using a combination of cryo-EM, biochemical assays, and quantitative nascent elongating transcript sequencing (qNET-seq), we establish that (p)ppGpp allosterically regulates pausing and nucleotide addition via distinct motions of the RNAP swivel module and both competes with and lowers GTP in vivo. (p)ppGpp stimulates swiveling at pause sites to delay escape but may also inhibit counter-swiveling required in every round of nucleotide addition. This repository stores the custom code accompanying this manuscript.

  PublisherDOI

• ppGpp regulates transcription elongation via direct and indirect inputs to RNA polymerase pausing and nucleotide addition

  Zenodo (CERN European Organization for Nuclear Research) · 2027-04-03

  articleOpen access1st authorCorresponding

  The signaling molecules guanosine 5′-tri/diphosphate 3′-diphosphate, (p)ppGpp, control bacterial protein synthesis rates and cell growth by targeting transcription, translation, NTP synthesis, and other functions. In lineages like E. coli, (p)ppGpp produced in response to charged-tRNA deficiency targets transcribing RNAP polymerase (RNAP) to match its pace to the pioneering ribosome on the nascent RNA (transcription–translation coupling). However, the mechanism by which (p)ppGpp slows RNAP is poorly defined. (p)ppGpp may allosterically stimulate RNAP pausing, inhibit catalysis, promote backtracking, compete for substrate GTP, inhibit GTP synthesis, or uncouple transcription–translation by inhibiting translation. Using a combination of cryo-EM, biochemical assays, and quantitative nascent elongating transcript sequencing (qNET-seq), we establish that (p)ppGpp allosterically regulates pausing and nucleotide addition via distinct motions of the RNAP swivel module and both competes with and lowers GTP in vivo. (p)ppGpp stimulates swiveling at pause sites to delay escape but may also inhibit counter-swiveling required in every round of nucleotide addition. This repository stores the custom code accompanying this manuscript.

  PublisherDOI

• Cell-free genomics reveals fundamental regulatory principles of the Mycobacterium tuberculosis transcription cycle

  Molecular Cell · 2026-02-01 · 1 citations

  articleOpen access
  PublisherOA PDFDOI

• RNA polymerase inhibitors reveal active-site motions essential for the nucleotide-addition cycle

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-04-07

  articleOpen access

  ABSTRACT The nucleotide-addition cycle (NAC) of multi-subunit DNA-dependent RNA polymerases (RNAPs) involves coordinated conformational changes in conserved active-site structural elements, including the trigger loop (TL). The TL is open (unfolded) in most RNAP structures but can close (fold) in substrate-bound (post- or pre-translocated) states of the RNAP, promoting catalysis. TL closure has been associated with closure of another conserved structural element, the Rim-Helices/F-loop (RH-FL), but the role of the RH-FL in the NAC is unclear. Antibiotic leads CBR9379 and AAP-SO 2 inhibit the Escherichia coli and Mycobacterium tuberculosis RNAPs, respectively, by binding in a pocket formed by the bridge helix and RH-FL. The precise mechanism of action for these inhibitors is yet to be defined. We present cryo-electron microscopy structures showing that both compounds inhibit the RNAP NAC by preventing RH-FL closure, thereby allosterically destabilizing the closed TL. This work reveals a conserved mechanistic principle of RNAP catalysis across all domains of life and provides new insight for antibiotic design.

  PublisherOA PDFDOI

• Harnessing evolution: leveraging bacterial isoprenoid pathway diversity toward improved bioengineering strategies

  Journal of Bacteriology · 2026-02-17

  articleOpen access

  Isoprenoids play vital roles in all domains of life, from beta-carotene in bacteria to heme in humans. Two distinct metabolic pathways have evolved to synthesize the critical precursor of all mature isoprenoids: the mevalonate (MEV) and the methylerythritol phosphate (MEP) pathways. Here, we quantify the extensive inter- and intra-genus heterogeneity in the usage of these two pathways with particular emphasis on rare bacteria that encode both, or neither, pathways. Furthermore, MEP intermediates themselves have non-isoprenogenic roles that may underlie evolutionary pressures driving pathway diversification. Understanding isoprenoid biosynthesis in bacteria offers new avenues toward more sustainable engineering of economically relevant molecules in microbes.

  PublisherDOI

• BPS2025 - Mechanisms and consequences of RNA duplex formation within the exit channel of RNA polymerases

  Biophysical Journal · 2025-02-01

  article
  PublisherDOI

• Cryo-EM of SARS-CoV-2 pre-incorporation replication-transcription complex with ATP

  EMPIAR dataset · 2025-03-06

  datasetOpen access
  PublisherDOI

• Cryo-EM of SARS-SoV-2 pre-incorporation replication-transcription complex with GTP

  EMPIAR dataset · 2025-03-13

  datasetOpen access

  EMPIAR, the Electron Microscopy Public Image Archive centered at EMBL-EBI, is a public resource for raw electron microscopy images related to EMDB, contains micrographs, particle sets and tilt-series.

  PublisherDOI

• Cryo-EM of SARS-CoV-2 pre-incorporation replication-transcription complex with CTP

  EMPIAR dataset · 2025-03-14

  datasetOpen access

  EMPIAR, the Electron Microscopy Public Image Archive centered at EMBL-EBI, is a public resource for raw electron microscopy images related to EMDB, contains micrographs, particle sets and tilt-series.

  PublisherDOI

Recent grants

• NIH Grant F32GM009151

  NIH · $25k

• NIH Grant R37GM038660

  NIH · $5.5M · 2011

• NIH Grant R01GM072795

  NIH · $775k · 2011

• NIH Grant R29GM038660

  NIH · $543k · 1992

• Structure/Function of Transcription Complex Regulation

  NIH · $13.3M · 1987–2027

Frequent coauthors

• Rachel A. Mooney

  77 shared

• Yaoping Zhang

  Southeast University

  76 shared

• Joshua J. Coon

  Morgridge Institute for Research

  72 shared

• Trey K. Sato

  Great Lakes Bioenergy Research Center

  69 shared

• Seth A. Darst

  50 shared

• Jessica M. Vera

  University of Wisconsin–Madison

  39 shared

• Alexander S. Hebert

  University of Wisconsin–Madison

  38 shared

• Patricia J. Kiley

  34 shared

Labs

• Robert Landick LabPI

Education

• Ph.D., Microbiology

  University of Wisconsin-Madison

  1990

• M.S., Microbiology

  University of Wisconsin-Madison

  1986

• B.S., Microbiology

  University of Wisconsin-Madison

  1984