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Rachel Green

· Bloomberg Distinguished Professor

Johns Hopkins University · Biochemistry and Molecular Biology

Active 1974–2025

h-index114
Citations37.5k
Papers463152 last 5y
Funding$43.2M

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

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About

Rachel Green received her B.S. in Chemistry at the University of Michigan in 1986. She performed her thesis work in biochemistry in 1993 in the laboratory of Jack Szostak at Harvard University, focusing on structural and functional analysis of catalytic RNAs and the implications of such molecules for the earliest evolution of life. As a postdoctoral fellow at UC Santa Cruz, she began her work on the ribosome with Harry Noller, exploring the diverse functions of rRNA and tRNA in translation. In 1998, she started as an assistant professor in the Department of Molecular Biology and Genetics at The Johns Hopkins University School of Medicine and was promoted to full professor in 2007. Since 2000, her work has been supported by the Howard Hughes Medical Institute (HHMI). Her laboratory focuses on diverse aspects of translation and its regulation in bacteria, yeast, and higher eukaryotic systems, with a recent emphasis on defining the molecular mechanisms that specify the high fidelity of protein synthesis during translation.

Research topics

  • Cell biology
  • Biology
  • Biochemistry
  • Genetics

Selected publications

  • Ribosome Collisions Trigger General Stress Responses to Regulate Cell Fate

    Cell · 2020 · 533 citations

    Senior authorCorresponding
  • EDF1 coordinates cellular responses to ribosome collisions

    eLife · 2020 · 187 citations

    Senior authorCorresponding

    Translation of aberrant mRNAs induces ribosomal collisions, thereby triggering pathways for mRNA and nascent peptide degradation and ribosomal rescue. Here we use sucrose gradient fractionation combined with quantitative proteomics to systematically identify proteins associated with collided ribosomes. This approach identified Endothelial differentiation-related factor 1 (EDF1) as a novel protein recruited to collided ribosomes during translational distress. Cryo-electron microscopic analyses of…

  • The ribotoxic stress response drives UV-mediated cell death

    Cell · 2024-06-05 · 96 citations

    articleOpen accessSenior authorCorresponding

    While ultraviolet (UV) radiation damages DNA, eliciting the DNA damage response (DDR), it also damages RNA, triggering transcriptome-wide ribosomal collisions and eliciting a ribotoxic stress response (RSR). However, the relative contributions, timing, and regulation of these pathways in determining cell fate is unclear. Here we use time-resolved phosphoproteomic, chemical-genetic, single-cell imaging, and biochemical approaches to create a chronological atlas of signaling events activated in ce…

  • RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks

    Molecular Cell · 2023-11-09 · 54 citations

    articleOpen access

    Reactive aldehydes are abundant endogenous metabolites that challenge homeostasis by crosslinking cellular macromolecules. Aldehyde-induced DNA damage requires repair to prevent cancer and premature aging, but it is unknown whether cells also possess mechanisms that resolve aldehyde-induced RNA lesions. Here, we establish photoactivatable ribonucleoside-enhanced crosslinking (PAR-CL) as a model system to study RNA crosslinking damage in the absence of confounding DNA damage in human cells. We fi…

  • LARP1 binds ribosomes and TOP mRNAs in repressed complexes

    The EMBO Journal · 2024-11-12 · 23 citations

    articleOpen accessSenior author

    Terminal oligopyrimidine motif-containing mRNAs (TOPs) encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies have implicated LARP1 in 40S- or 80S-ribosome complexes that are thought to repress and stabilize TOPs. However, a molecular understanding of how LARP1 and TOPs interact with these ribosome complexes is lacking. Here, we show that LARP1 directly binds non-translating ribosomal subunits. Cryo-EM structures reveal a previously…

Recent grants

Frequent coauthors

  • Boris Zinshteyn

    Johns Hopkins University

    94 shared
  • Julie L Brunelle

    Howard Hughes Medical Institute

    91 shared
  • Colin Chih‐Chien Wu

    Center for Cancer Research

    78 shared
  • Allen R. Buskirk

    Johns Hopkins University

    73 shared
  • Niladri K. Sinha

    Johns Hopkins University

    63 shared
  • Jamie R Wangen

    Howard Hughes Medical Institute

    50 shared
  • Daniel Goldman

    Western University

    48 shared
  • Laura N. Lessen

    Howard Hughes Medical Institute

    48 shared

Labs

Awards & honors

  • Supported by Howard Hughes Medical Institute (since 2000)

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