Sylvie Doublié

Sylvie Doublié
Alma materUniversity of Paris
Scientific career
FieldsBiochemistry, X-ray crystallography, DNA Repair
InstitutionsUniversity of Paris
University of North Carolina at Chapel Hill
European Molecular Biology Laboratory, Grenoble
Harvard Medical School
University of Vermont
Thesis2.9 angstrom crystal structure of Bacillus stearothermophilus tryptophanyl-tRNA synthetase complexed to its adenylate, tryptophanyl-5'AMP (1993)
Doctoral advisorsCharles W. Carter, Jr.
Other academic advisorsStephen A. Cusack
Tom Ellenberger
WebsiteUniversity of Vermont, Sylvie Doublié

Sylvie Doublié is the Green and Gold Professor in the Department of Microbiology and Molecular Genetics at the University of Vermont Robert Larner College of Medicine.[1][2] Doublié is a structural biologist and biochemist who has worked on DNA replication, DNA repair, and messenger RNA (mRNA) processing. She is an elected member (2013) of the Vermont Academy of Sciences and a member of the academy's board of directors.[3][4]

Education and career

Doublié received B.S. (Biological Sciences) and M.Sci. (Biochemistry) degrees (1985) from Paris-East Créteil University, and an advanced degree (Biological Crystallography, 1988) at Paris-Sud University, Orsay. She received a Ph.D. (Biochemistry and Biophysics, 1993) at the University of North Carolina at Chapel Hill, followed by postdoctoral work at the European Molecular Biology Laboratory in Grenoble, France and then at Harvard Medical School.[5]

After joining the Robert Larner College of Medicine at the University of Vermont in 1998, Doublié was awarded a Pew Biomedical Scholarship (2000) from The Pew Charitable Trusts.[6] She now holds the inaugural endowed Green and Gold Professorship in the Department of Microbiology and Molecular Genetics.[2]

Research

Doublié's research includes the high-resolution crystal structure of T7 DNA polymerase with DNA and nucleotide.[7][8] She obtained an initial structure of a replicative DNA polymerase bound to an abasic site, allowing visualization of intermediate steps as DNA travels from the polymerase to the proofreading site.[9] She was the earliest to solve a crystal structure of a mammalian poly(A) polymerase for mRNA.[10] Her work on mammalian mRNA cleavage factor Im (CFIm) provided insight into RNA recognition, RNA looping and the role of CFIm in alternative polyadenylation.[11] She solved the crystal structures of several DNA glycosylase enzymes that scan the genome, recognizing and excising damaged DNA bases specifically among a sea of normal bases. Doublié's research group determined the crystal structure of any endonuclease VIII family glycosylase bound to an oxidized DNA lesion.[12] The work showed that in this class of enzymes, lesion recognition happens before the damaged base is everted. She obtained the initial structure of the polymerase domain of the human DNA repair enzyme DNA polymerase θ.[13] This showed that lesion bypass activity is linked to the ability of the polymerase to grip the primer 3’ end tightly.[14] Her description of methods for selenomethionine substitution in structure determination by X-ray crystallography is highly cited.[15] Doublié edited a two-volume book series on protocols for macromolecular crystallography.[16]

Honors and Selected Positions

References

  1. ^ "Sylvie Doublié, Ph.D.: Professor". Retrieved 2 December 2025.
  2. ^ a b "Investiture of Sylvie Doublié, Ph.D." Retrieved 15 December 2025.
  3. ^ a b "Sylvie Doublié | Vermont Academy of Science & Engineering". VASE (new). Retrieved 17 December 2025.
  4. ^ "VASE Board of Directors". Retrieved 2 December 2025.
  5. ^ Caruso, David J. "Oral history interview with Sylvie Doublié, 2008-Nov-05 – 2008-Nov-06". Science History Institute Museum & Library, Digital Collections. Retrieved 2025-12-26.
  6. ^ a b "Sylvie Doublié, Ph.D." bit.ly. Retrieved 17 December 2025.
  7. ^ Doublié, S.; Tabor, S.; Long, A. M.; Richardson, C. C.; Ellenberger, T. (15 January 1998). "Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution". Nature. 391 (6664): 251–258. doi:10.1038/34593. ISSN 0028-0836.
  8. ^ Steitz, Thomas A. (1998-01-15). "A mechanism for all polymerases". Nature. 391 (6664): 231–232. doi:10.1038/34542. ISSN 1476-4687.
  9. ^ Hogg, Matthew; Wallace, Susan S.; Doublié, Sylvie (7 April 2004). "Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site". The EMBO Journal. 23 (7): 1483–1493. doi:10.1038/sj.emboj.7600150. ISSN 0261-4189. PMID 15057283. Retrieved 17 December 2025.
  10. ^ Martin, G.; Keller, W.; Doublié, S. (15 August 2000). "Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP". The EMBO Journal. 19 (16): 4193–4203. doi:10.1093/emboj/19.16.4193. ISSN 0261-4189. PMC 302044. PMID 10944102. Retrieved 17 December 2025.
  11. ^ Graveley, Brenton R. (2011-03-09). "Getting in the Loop: New Insights into the Mechanism of Poly(A) Site Recognition". Structure. 19 (3): 279–281. doi:10.1016/j.str.2011.02.005. ISSN 0969-2126. PMID 21397179.
  12. ^ Doublié, Sylvie; Bandaru, Viswanath; Bond, Jeffrey P.; Wallace, Susan S. (13 July 2004). "The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity". Proceedings of the National Academy of Sciences of the United States of America. 101 (28): 10284–10289. doi:10.1073/pnas.0402051101. ISSN 0027-8424. PMID 15232006.
  13. ^ Daniels, Kendall (November 15, 2023). "Scientists Piece Together DNA Repair Pathway Implicated in Breast, Ovarian, and Prostate Cancers". UNC Health and UNC School of Medicine Newsroom.
  14. ^ Beard, William A.; Wilson, Samuel H. (2015-04-03). "Structures of human DNA polymerases ν and θ expose their end game". Nature Structural & Molecular Biology. 22 (4): 273–275. doi:10.1038/nsmb.3006. ISSN 1545-9985.
  15. ^ "Sylvie Doublie". scholar.google.com. Retrieved 2025-12-26.
  16. ^ Doublié, Sylvie, ed. (2007). Macromolecular Crystallography Protocols. Humana Press.
  17. ^ "Sylvie Doublié, NIEHS". Retrieved 17 December 2025.
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