Danesh Moazed

Danesh Moazed, Ph.D.

Professor of Cell Biology (HMS)
HHMI Investigator

Danesh Moazed, Ph.D., is a Professor and HHMI Investigator in the Department of Cell Biology at Harvard Medical School.  He is a member of the Harvard Biophysics Program and the Harvard Initiative for RNA Medicine (HIRM). He received his undergraduate and Ph.D. degrees from the University of California in Santa Cruz and performed postdoctoral studies at the University of California in San Francisco.

The Moazed lab studies how genes are silenced and how silencing is epigenetically inherited across generations.  The lab’s interests revolve around diverse pathways of heterochromatin-mediated gene silencing in yeast and mammalian cells.  Work in budding yeast focuses on the structure and function of a diverged and relatively simple form of heterochromatin, which requires only three Silent information regulator (“Sir”) proteins that form a histone deacetylase and chromatin-binding complex.  Work in fission yeast focuses on a conserved example of heterochromatin that requires the nuclear RNA interference (RNAi) machinery, other RNA processing pathways, Heterochromatin protein 1 (HP1) homologs, and histone-modifying enzymes.  In mammalian cells, the work is focused on HP1-mediated and other heterochromatin formation pathways.  The lab uses approaches ranging from genetics and genomics, biochemical purification and reconstitution, and structural biology for their studies.  Ultimately, the lab seeks to understand the conserved fundamental principles that govern the assembly, function, and epigenetic propagation of heterochromatin.

Harvard Medical School

Dept. of Cell Biology, SGM 402B

240 Longwood Avenue

Boston, MA 02115

Lab telephone: 617-432-1258

Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation.
Authors: Authors: Li J, Moazed D, Gygi SP.
J Biol Chem
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Recognition of acetylated proteins: lessons from an ancient family of enzymes.
Authors: Authors: Tanny JC, Moazed D.
Structure
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Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a Sir2/Sir4 complex to silencers and role for Sir2-dependent deacetylation.
Authors: Authors: Hoppe GJ, Tanny JC, Rudner AD, Gerber SA, Danaie S, Gygi SP, Moazed D.
Mol Cell Biol
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Protein- and immunoaffinity purification of multiprotein complexes.
Authors: Authors: Kellogg DR, Moazed D.
Methods Enzymol
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Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening.
Authors: Authors: Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL.
J Biol Chem
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Common themes in mechanisms of gene silencing.
Authors: Authors: Moazed D.
Mol Cell
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Net1 stimulates RNA polymerase I transcription and regulates nucleolar structure independently of controlling mitotic exit.
Authors: Authors: Shou W, Sakamoto KM, Keener J, Morimoto KW, Traverso EE, Azzam R, Hoppe GJ, Feldman RM, DeModena J, Moazed D, Charbonneau H, Nomura M, Deshaies RJ.
Mol Cell
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Enzymatic activities of Sir2 and chromatin silencing.
Authors: Authors: Moazed D.
Curr Opin Cell Biol
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Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product.
Authors: Authors: Tanny JC, Moazed D.
Proc Natl Acad Sci U S A
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An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing.
Authors: Authors: Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D.
Cell
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