Robert Lee

About

Robert Lee is an Associate Arts Professor and Associate Chair at NYU Tisch School of the Arts. He is a lyricist and librettist with a background in musical theatre writing. Lee and composer Leon Ko received a Richard Rodgers Development Award for their musical Heading East and an AT&T First Stage Grant for their musical Chinese Hell, developed with producer Margo Lion and San Francisco’s American Conservatory Theater. A 2010 concert staging of Heading East was the first musical presented at New York’s Asia Society. His other projects with Ko include a musical stage adaptation of Jean Kerr’s Please Don’t Eat the Daisies, developed with East of Doheny and La Jolla Playhouse, and the original musical Takeaway, which opened in London’s Theatre Royal Stratford East in 2011 and is notable for being the first major musical in the UK to address the British East Asian experience. Lee also contributed songs for the film Love is a Broadway Hit and co-created Alice Chan, a play for young audiences, with BD Wong for La Jolla Playhouse. Currently, he is adapting Chinese Hell into an animated web series called Chinese Hell—The Doodle Edition. Lee is an alumnus of Princeton University and the Graduate Musical Theatre Writing Program at NYU Tisch, where he is a full-time faculty member. He has served as a visiting professor at Princeton’s Lewis Center for the Arts and has been involved in various theatre projects and workshops, including the Stratford East Musical Theatre Writing Workshop…

Research topics

• Cell biology
• Biology
• Genetics
• Chemistry
• Biochemistry
• Cancer research

Selected publications

• Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation

  Science · 2021 · 115 citations

  Dot1 (disruptor of telomeric silencing-1), the histone H3 lysine 79 (H3K79) methyltransferase, is conserved throughout evolution, and its deregulation is found in human leukemias. Here, we provide evidence that acetylation of histone H4 allosterically stimulates yeast Dot1 in a manner distinct from but coordinating with histone H2B ubiquitination (H2BUb). We further demonstrate that this stimulatory effect is specific to acetylation of lysine 16 (H4K16ac), a modification central to chromatin str…

  PublisherOA PDFDOI

• The structure of a virus-encoded nucleosome

  Nature Structural & Molecular Biology · 2021 · 74 citations

  PublisherOA PDFDOI

• Structural basis of histone H2A lysine 119 deubiquitination by Polycomb repressive deubiquitinase BAP1/ASXL1

  Science Advances · 2023 · 49 citations

  Histone H2A lysine 119 (H2AK119Ub) is monoubiquitinated by Polycomb repressive complex 1 and deubiquitinated by Polycomb repressive deubiquitinase complex (PR-DUB). PR-DUB cleaves H2AK119Ub to restrict focal H2AK119Ub at Polycomb target sites and to protect active genes from aberrant silencing. The PR-DUB subunits (BAP1 and ASXL1) are among the most frequently mutated epigenetic factors in human cancers. How PR-DUB establishes specificity for H2AK119Ub over other nucleosomal ubiquitination sites…

  PublisherOA PDFDOI

• A giant virus genome is densely packaged by stable nucleosomes within virions

  Molecular Cell · 2022-11-11 · 37 citations

  articleOpen access

  The two doublet histones of Marseillevirus are distantly related to the four eukaryotic core histones and wrap 121 base pairs of DNA to form remarkably similar nucleosomes. By permeabilizing Marseillevirus virions and performing genome-wide nuclease digestion, chemical cleavage, and mass spectrometry assays, we find that the higher-order organization of Marseillevirus chromatin fundamentally differs from that of eukaryotes. Marseillevirus nucleosomes fully protect DNA within virions as closely a…

  PublisherDOI

• Cancer-associated DNA hypermethylation of Polycomb targets requires DNMT3A dual recognition of histone H2AK119 ubiquitination and the nucleosome acidic patch

  Science Advances · 2024-08-28 · 22 citations

  articleOpen access

  During tumor development, promoter CpG islands that are normally silenced by Polycomb repressive complexes (PRCs) become DNA-hypermethylated. The molecular mechanism by which de novo DNA methyltransferase(s) [DNMT(s)] catalyze CpG methylation at PRC-regulated regions remains unclear. Here, we report a cryo-electron microscopy structure of the DNMT3A long isoform (DNMT3A1) amino-terminal region in complex with a nucleosome carrying PRC1-mediated histone H2A lysine-119 monoubiquitination (H2AK119U…

  PublisherDOI

Frequent coauthors

• Karim‐Jean Armache

  New York University

  10 shared

• Evgeny Nudler

  Howard Hughes Medical Institute

  9 shared

• Pablo De Ioannes

  New York University

  8 shared

• Stephen Abini-Agbomson

  New York University

  8 shared

• Bernard La Scola

  Aix-Marseille Université

  7 shared

• Kristjan H. Gretarsson

  Columbia University Irving Medical Center

  6 shared

• Chao Lü

  Columbia University Irving Medical Center

  6 shared

• Marco Igor Valencia‐Sánchez

  New York University

  6 shared

Awards & honors

• Richard Rodgers Development Award
• AT&T First Stage Grant

Similar researchers at New York University

• Jonathan Bernsteinh-44
• Danny Haengil Larsenh-9
• Mindi Dicksteinh-8