Robert G. Roeder

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Robert G. Roeder
Robert G Roeder.jpg
Born
Robert Gayle Roeder

(1942-06-03) June 3, 1942 (age 82)
Boonville, Indiana, United States
NationalityAmerican
Alma mater University of Washington, University of Illinois, Wabash College
Known for
Awards
Scientific career
Fields
Institutions Washington University in St. Louis
Rockefeller University
Thesis Multiple RNA Polymerases and RNA Synthesis in Eukaryotic Systems  (1969)
Doctoral advisor William J. Rutter
Other academic advisors Donald D. Brown
Doctoral students

Robert G. Roeder (born June 3, 1942, in Boonville, Indiana, United States) is an American biochemist. He is known as a pioneer scientist in eukaryotic transcription. He discovered three distinct nuclear RNA polymerases in 1969 [1] and characterized many proteins involved in the regulation of transcription, including basic transcription factors and the first mammalian gene-specific activator over five decades of research. [2] He is the recipient of the Gairdner Foundation International Award in 2000, the Albert Lasker Award for Basic Medical Research in 2003, and the Kyoto Prize in 2021. He currently serves as Arnold and Mabel Beckman Professor and Head of the Laboratory of Biochemical and Molecular Biology at The Rockefeller University.

Contents

Biography

Roeder was born in Boonville, Indiana, US in 1942. He received his B.A. summa cum laude in chemistry from Wabash College in 1964 and his M.S. in chemistry from the University of Illinois in 1965. He received his Ph.D. in biochemistry in 1969 from the University of Washington, Seattle, where he worked with William J. Rutter. He did postdoctoral work with Donald D. Brown at the Carnegie Institution of Washington, in Baltimore, from 1969 to 1971. He was a member of the faculty at Washington University School of Medicine in St. Louis from 1971 to 1982, when he joined The Rockefeller University. In 1985, he was named Arnold and Mabel Beckman Professor. He was elected as a member of the National Academy of Sciences in 1988 and the American Academy of Arts and Sciences in 1995, and a foreign associate member of the European Molecular Biology Organization in 2003.

Major scientific discoveries

Highly cited papers

  1. Dignam, J. D.; Lebovitz, R. M.; Roeder, R. G. (March 11, 1983). "Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei". Nucleic Acids Research. 11 (5). Oxford University Press (OUP): 1475–1489. doi:10.1093/nar/11.5.1475. ISSN   0305-1048. PMC   325809 . PMID   6828386. Times Cited: 12,743
  2. Gu, Wei; Roeder, Robert G (1997). "Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain". Cell. 90 (4). Elsevier BV: 595–606. doi: 10.1016/s0092-8674(00)80521-8 . ISSN   0092-8674. PMID   9288740. S2CID   18434280. Times Cited: 3,236
  3. Roeder, Robert G (1996). "The role of general initiation factors in transcription by RNA polymerase II". Trends in Biochemical Sciences. 21 (9). Elsevier BV: 327–335. doi:10.1016/S0968-0004(96)10050-5. ISSN   0968-0004. PMID   8870495. Times Cited: 1,511
  4. Sawadogo, M (1985). "Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region". Cell. 43 (1). Elsevier BV: 165–175. doi:10.1016/0092-8674(85)90021-2. ISSN   0092-8674. PMID   4075392. S2CID   42562115.Times Cited: 1,377
  5. Roeder, Robert G.; Rutter, William J. (1969). "Multiple Forms of DNA-dependent RNA Polymerase in Eukaryotic Organisms". Nature. 224 (5216). Springer Science and Business Media LLC: 234–237. Bibcode:1969Natur.224..234R. doi:10.1038/224234a0. ISSN   0028-0836. PMID   5344598. S2CID   4283528. Times Cited: 1,177

Honors and awards

Prominent alumni of the Roeder Laboratory

The Roeder Laboratory has trained hundreds of students and postdoctoral fellows, many of whom hold independent positions in prominent biomedical research institutions, including Richard A. Bernstein (Northwestern University), Robert B. Darnell (Rockefeller University and HHMI), Beverly M. Emerson (Salk Institute for Biological Studies), Michael R. Green (University of Massachusetts Medical School and HHMI), Wei Gu (Columbia University), Nathaniel Heintz (Rockefeller University and HHMI), Andrew B. Lassar (Harvard Medical School), Carl S. Parker (California Institute of Technology), Ron Prywes (Columbia University), Danny Reinberg (New York University School of Medicine and HHMI), Hazel L. Sive (Massachusetts Institute of Technology and Whitehead Institute) and Jerry Workman (Stowers Institute for Medical Research). [37]

Related Research Articles

<span class="mw-page-title-main">RNA polymerase II</span> Protein complex that transcribes DNA

RNA polymerase II is a multiprotein complex that transcribes DNA into precursors of messenger RNA (mRNA) and most small nuclear RNA (snRNA) and microRNA. It is one of the three RNAP enzymes found in the nucleus of eukaryotic cells. A 550 kDa complex of 12 subunits, RNAP II is the most studied type of RNA polymerase. A wide range of transcription factors are required for it to bind to upstream gene promoters and begin transcription.

<span class="mw-page-title-main">TATA-binding protein</span> Protein-coding gene in the species Homo sapiens

The TATA-binding protein (TBP) is a general transcription factor that binds to a DNA sequence called the TATA box. This DNA sequence is found about 30 base pairs upstream of the transcription start site in some eukaryotic gene promoters.

Transcription factor II D (TFIID) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex. RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells. It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins. Before the start of transcription, the transcription Factor II D (TFIID) complex binds to the core promoter DNA of the gene through specific recognition of promoter sequence motifs, including the TATA box, Initiator, Downstream Promoter, Motif Ten, or Downstream Regulatory elements.

<span class="mw-page-title-main">TAF6</span> Protein-coding gene in the species Homo sapiens

Transcription initiation factor TFIID subunit 6 is a protein that in humans is encoded by the TAF6 gene.

<span class="mw-page-title-main">TAF1</span> Protein-coding gene in the species Homo sapiens

Transcription initiation factor TFIID subunit 1, also known as transcription initiation factor TFIID 250 kDa subunit (TAFII-250) or TBP-associated factor 250 kDa (p250), is a protein that in humans is encoded by the TAF1 gene.

<span class="mw-page-title-main">MED1</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 1 also known as DRIP205 or Trap220 is a subunit of the Mediator complex and is a protein that in humans is encoded by the MED1 gene. MED1 functions as a nuclear receptor coactivator.

<span class="mw-page-title-main">TAF9</span> Protein-coding gene in the species Homo sapiens

TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa, also known as TAF9, is a protein that in humans is encoded by the TAF9 gene.

<span class="mw-page-title-main">TCEA1</span> Human protein-coding gene

Transcription elongation factor A protein 1 is a protein that in humans is encoded by the TCEA1 gene.

<span class="mw-page-title-main">SUB1</span> Protein-coding gene in the species Homo sapiens

Activated RNA polymerase II transcriptional coactivator p15 also known as positive cofactor 4 (PC4) or SUB1 homolog is a protein that in humans is encoded by the SUB1 gene. The human SUB1 gene is named after an orthologous gene in yeast.

<span class="mw-page-title-main">Cyclin-dependent kinase 8</span> Protein-coding gene in the species Homo sapiens

Cell division protein kinase 8 is an enzyme that in humans is encoded by the CDK8 gene.

<span class="mw-page-title-main">TAF10</span> Protein-coding gene in the species Homo sapiens

Transcription initiation factor TFIID subunit 10 is a protein that in humans is encoded by the TAF10 gene.

<span class="mw-page-title-main">TAF5</span> Protein-coding gene in the species Homo sapiens

Transcription initiation factor TFIID subunit 5 is a protein that in humans is encoded by the TAF5 gene.

<span class="mw-page-title-main">MED24</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 24 is an enzyme that in humans is encoded by the MED24 gene.

<span class="mw-page-title-main">MED4</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 4 also known as mediator complex subunit 4 (MED4), a component of Mediator or vitamin D3 receptor-interacting protein complex 36 kDa component (DRIP36) is a protein that in humans is encoded by the MED4 gene.

<span class="mw-page-title-main">GTF3A</span> Protein-coding gene in the species Homo sapiens

Transcription factor IIIA is a protein that in humans is encoded by the GTF3A gene.

<span class="mw-page-title-main">MED17</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 17 is an enzyme that in humans is encoded by the MED17 gene.

<span class="mw-page-title-main">TAF6L</span> Protein-coding gene in the species Homo sapiens

TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L is an enzyme that in humans is encoded by the TAF6L gene.

<span class="mw-page-title-main">GTF2F1</span> Protein-coding gene in the species Homo sapiens

General transcription factor IIF subunit 1 is a protein that in humans is encoded by the GTF2F1 gene.

<span class="mw-page-title-main">MED26</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 26 is an enzyme that in humans is encoded by the MED26 gene. It forms part of the Mediator complex.

The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). TADs are named after their amino acid composition. These amino acids are either essential for the activity or simply the most abundant in the TAD. Transactivation by the Gal4 transcription factor is mediated by acidic amino acids, whereas hydrophobic residues in Gcn4 play a similar role. Hence, the TADs in Gal4 and Gcn4 are referred to as acidic or hydrophobic, respectively.

References

  1. 1 2 Roeder RG, Rutter WJ (October 1969). "Multiple forms of DNA-dependent RNA polymerase in eukaryotic organisms". Nature. 224 (5216): 234–7. Bibcode:1969Natur.224..234R. doi:10.1038/224234a0. PMID   5344598. S2CID   4283528.
  2. ↑ Roeder RG (September 2019). "50+ years of eukaryotic transcription: an expanding universe of factors and mechanisms". Nature Structural & Molecular Biology. 26 (9): 783–791. doi:10.1038/s41594-019-0287-x. PMC   6867066 . PMID   31439941.
  3. ↑ Sklar VE, Schwartz LB, Roeder RG (January 1975). "Distinct molecular structures of nuclear class I, II and III DNA-dependent RNA polymerases". Proc Natl Acad Sci U S A. 72 (1): 348–52. Bibcode:1975PNAS...72..348S. doi: 10.1073/pnas.72.1.348 . PMC   432302 . PMID   1054509.
  4. ↑ Reeder RH, Roeder RG (June 1972). "Ribosomal RNA synthesis in isolated nuclei". J Mol Biol. 67 (3): 433–41. doi:10.1016/0022-2836(72)90461-5. PMID   4558099.
  5. ↑ Weinmann R, Roeder RG (May 1974). "Role of DNA-Dependent RNA Polymerase III in the Transcription of the tRNA and 5S RNA Genes". Proc Natl Acad Sci U S A. 71 (5): 1790–4. Bibcode:1974PNAS...71.1790W. doi: 10.1073/pnas.71.5.1790 . PMC   388326 . PMID   4525293.
  6. ↑ Weinmann R, Raskas HJ, Roeder RG (September 1974). "Role of DNA-Dependent RNA Polymerases II and III in Transcription of the Adenovirus Genome Late in Productive Infection". Proc Natl Acad Sci U S A. 71 (9): 3426–39. Bibcode:1974PNAS...71.3426W. doi: 10.1073/pnas.71.9.3426 . PMC   433786 . PMID   4530313.
  7. ↑ Parker CS, Roeder RG (January 1977). "Selective and accurate transcription of the Xenopus laevis 5S RNA genes in isolated chromatin by purified RNA polymerase III". Proc Natl Acad Sci U S A. 74 (1): 44–8. Bibcode:1977PNAS...74...44P. doi: 10.1073/pnas.74.1.44 . PMC   393193 . PMID   264693.
  8. ↑ Ng SY, Parker CS, Roeder RG (January 1979). "Transcription of cloned Xenopus 5S RNA genes by X. laevis RNA polymerase III in reconstituted systems". Proc Natl Acad Sci U S A. 76 (1): 136–40. Bibcode:1979PNAS...76..136N. doi: 10.1073/pnas.76.1.136 . PMC   382891 . PMID   284325.
  9. ↑ Weil PA, Luse DS, Segall J, Roeder RG (October 1979). "Selective and accurate initiation of transcription at the Ad2 major late promotor in a soluble system dependent on purified RNA polymerase II and DNA". Cell. 18 (2): 469–84. doi:10.1016/0092-8674(79)90065-5. PMID   498279. S2CID   34095322.
  10. ↑ Parker CS, Jaehning JA, Roeder RG (1978). "Faithful gene transcription by eukaryotic RNA polymerases in reconstructed systems". Cold Spring Harb Symp Quant Biol. 42 (1): 577–87. doi:10.1101/sqb.1978.042.01.060. PMID   277365.
  11. ↑ Segall J, Matsui T, Roeder RG (December 1980). "Multiple factors are required for the accurate transcription of purified genes by RNA polymerase III". J Biol Chem. 255 (24): 11986–91. doi: 10.1016/S0021-9258(19)70231-2 . PMID   7440579.
  12. ↑ Matsui T, Segall J, Weil PA, Roeder RG (December 1980). "Multiple factors required for accurate initiation of transcription by purified RNA polymerase II". J Biol Chem. 255 (24): 11992–6. doi: 10.1016/S0021-9258(19)70232-4 . PMID   7440580.
  13. ↑ Roeder RG, Engelke DR, Luse DS, Segall J, Shastry BS, Weil PA (1979). "Factors involved in the transcription of purified genes by RNA polymerase III". ICN-UCLA Symposium on Gene Regulation in Eukaryote. eds. R. Axel and T. Maniatis. Academic Press, New York: 521–540.
  14. ↑ Engelke DR, Ng SY, Shastry BS, Roeder RG (March 1980). "Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes". Cell. 19 (3): 717–28. doi:10.1016/S0092-8674(80)80048-1. PMID   6153931. S2CID   23955175.
  15. ↑ Meisterernst M, Roy AL, Lieu HM, Roeder RG (September 1991). "Activation of class II gene transcription by regulatory factors is potentiated by a novel activity". Cell. 66 (5): 981–93. doi:10.1016/0092-8674(91)90443-3. PMID   1889091. S2CID   43608887.
  16. ↑ Ge H, Roeder RG (August 1994). "Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes". Cell. 78 (3): 513–23. doi:10.1016/0092-8674(94)90428-6. PMID   8062391. S2CID   1140379.
  17. ↑ Luo Y, Fujii H, Gerster T, Roeder RG (October 1992). "A novel B cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors". Cell. 71 (2): 231–41. doi:10.1016/0092-8674(92)90352-D. PMID   1423591. S2CID   24583386.
  18. ↑ Fondell JD, Ge H, Roeder RG (August 1996). "Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex". Proc Natl Acad Sci U S A. 93 (16): 8329–33. Bibcode:1996PNAS...93.8329F. doi: 10.1073/pnas.93.16.8329 . PMC   38670 . PMID   8710870.
  19. ↑ Ge K, Guermah M, Yuan CX, Ito M, Wallberg AE, Spiegelman BM, Roeder RG (May 2002). "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis". Nature. 417 (6888): 563–7. Bibcode:2002Natur.417..563G. doi:10.1038/417563a. PMID   12037571. S2CID   4432077.
  20. ↑ ACS Biological Chemistry: Achievement and Travel Awards
  21. ↑ National Academy of Sciences Award in Molecular Biology
  22. ↑ Lewis S. Rosenstiel Award Archived July 25, 2008, at the Wayback Machine
  23. ↑ The Passano Foundation
  24. ↑ The Official Site of Louisa Gross Horwitz Prize
  25. ↑ Volkers, N. (July 7, 1999). "General Motors Cancer Research Foundation Awards Honor Top Cancer Innovators". JNCI Journal of the National Cancer Institute. 91 (13): 1107–1108. doi:10.1093/jnci/91.13.1107. ISSN   0027-8874. PMID   10393714.
  26. ↑ The Gairdner Foundation
  27. ↑ Science 2001 Dickson Prize Lecturer Archived June 26, 2007, at the Wayback Machine
  28. ↑ ASBMB-Merck Award [ permanent dead link ]
  29. ↑ The Lasker Foundation
  30. ↑ McGinn, Susan Killenberg (May 5, 2005). "Washington University to confer five honorary degrees May 20 – The Source – Washington University in St. Louis". The Source. Retrieved August 11, 2023.
  31. ↑ "Salk Institute Medals to be awarded to Pioneering Biologist Robert Roeder and High-Tech Innovator/Philanthropist Irwin Jacobs". Salk Institute for Biological Studies. Retrieved August 11, 2023.
  32. ↑ "'Towering Figures' in Cell Research to Share Albany Medical Center Prize". Archived from the original on October 2, 2015. Retrieved April 14, 2012.
  33. ↑ "Roeder 'a consumate biochemist and absolute perfect fit' for the honor". www.asbmb.org. Retrieved August 11, 2023.
  34. ↑ "105th Howard Taylor Ricketts Lecture -"Transcriptional regulatory mechanisms in animal cells" – University of Chicago – Department of Medicine". medicine.uchicago.edu. Retrieved August 11, 2023.
  35. ↑ "Shizhang Bei International Award". en.bsc.org.cn. Retrieved August 11, 2023.
  36. ↑ 2021 Kyoto Prize Laureates – Discovery of the Principle of Gene Transcription Mechanisms in Eukaryotes
  37. ↑ Abmayr SM, Workman JL (October 2003). "Transcription factors prominently in Lasker Award to Roeder". Cell. 115 (3): 243–6. doi: 10.1016/S0092-8674(03)00846-8 . PMID   14636549. S2CID   17097436.
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