Paul W. Huber

Paul W. Huber received the B.S. degree in biology and chemistry from Boston College in 1973. In 1978, he earned the Ph.D. degree in biochemistry at Purdue University followed by postdoctoral studies at the University of Chicago. During this time, he became interested in RNA structure and RNA-protein interactions. He continued this research when he took a faculty position at the University of Notre Dame in 1985. Much of his work has focused on two proteins, transcription factor IIIA (TFIIIA) and ribosomal protein L5, that have mutually exclusive binding sites on 5S ribosomal RNA. These two proteins are the mediators of 5S rRNA metabolism in oocytes. This work has encompassed biochemical, biophysical, and molecular biological studies. More recently, the attention of his research group has turned to RNA localization during Xenopus oogenesis. Dr. Huber’s group has identified three proteins that bind to the localization element of Vg1 mRNA and are currently studying the function of these proteins in process of localization. Dr. Huber has served on study sections for the National Institutes of Health and the American Heart Association. He has served as a reviewer for numerous scientific journals and other funding agencies, including the National Science Foundation, the Wellcome Trust, and the Israel Science Foundation among others. Dr. Huber holds the rank of Professor in the Department of Chemistry and Biochemistry at Notre Dame and was a Visiting Fellow in 1997 at Yale University.

Biography Updated on 29 August 2007

Articles in Scholarly Journals [Incomplete List]

  1. Langmuir, vol. 22, no. 26, pp. 11279–11283, 2006
  2. Restricted Specificity of Xenopus TFIIIA for Transcription of Somatic 5S rRNA Genes
    Molecular and Cellular Biology, vol. 24, no. 6, pp. 2467–2477, 2004
  3. Mutual Induced Fit Binding of Xenopus Ribosomal Protein L5 to 5S rRNA
    Journal of Molecular Biology, vol. 330, no. 5, pp. 979–992, 2003
  4. VgRBP71 Stimulates Cleavage at a Polyadenylation Signal in Vg1 mRNA, Resulting in the Removal of a cis-Acting Element that Represses Translation
    Molecular Cell, vol. 11, no. 3, pp. 745–755, 2003
  5. Phosphorylation of Xenopus transcription factor IIIA by an oocyte protein kinase CK2
    Biochemical Journal, vol. 362, no. 2, p. 375, 2002
  6. A homolog of FBP2/KSRP binds to localized mRNAs in Xenopus oocytes
    Development, vol. 129, no. 24, pp. 5609–5619, 2002
  7. A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization
    The EMBO Journal, vol. 20, no. 9, pp. 2315–2325, 2001
  8. Biochemistry, vol. 40, no. 42, pp. 12645–12653, 2001
  9. The structure of helix III in Xenopus oocyte 5 S rRNA: an RNA stem containing a two-nucleotide bulge,
    Journal of Molecular Biology, vol. 312, no. 4, pp. 823–832, 2001
  10. Biochemistry, vol. 37, no. 16, pp. 5549–5557, 1998
  11. Inhibition of RNA polymerase III transcription by a ribosome-associated kinase activity
    Nucleic Acids Research, vol. 26, no. 20, pp. 4758–4764, 1998
  12. Analysis of the Binding of Xenopus Transcription Factor IIIA to Oocyte 5 S rRNA and to the 5 S rRNA Gene
    Journal of Biological Chemistry, vol. 271, no. 2, pp. 869–877, 1996
  13. Analysis of the Binding of Xenopus Ribosomal Protein L5 to Oocyte 5 S rRNA
    Journal of Biological Chemistry, vol. 270, no. 45, pp. 27358–27365, 1995
  14. Synthesis, bioactivity, and DNA-cleaving ability of desferrioxamine B-nalidixic acid and anthraquinone carboxylic acid conjugates
    Bioorganic & Medicinal Chemistry Letters, vol. 5, no. 20, pp. 2337–2340, 1995
  15. Biochemistry, vol. 31, no. 13, pp. 3534–3542, 1992
  16. Structural Polymorphism in the Major Groove of a 5S RNA Gene Complements the Zinc Finger Domains of Transcription Factor IIIA
    Proceedings of the National Academy of Sciences, vol. 88, no. 23, pp. 10801–10805, 1991
  17. Identification of the Binding Site on 5S rRNA for the Transcription Factor IIIA: Proposed Structure of a Common Binding Site on 5S rRNA and on the Gene
    Proceedings of the National Academy of Sciences, vol. 83, no. 6, pp. 1593–1597, 1986
  18. Nuclease Protection Analysis of Ribonucleoprotein Complexes: Use of the Cytotoxic Ribonuclease alpha -sarcin to Determine the Binding Sites for Escherichia coli Ribosomal Proteins L5, L18, and L25 on 5S rRNA
    Proceedings of the National Academy of Sciences, vol. 81, no. 2, pp. 322–326, 1984
  19. Biochemistry, vol. 19, no. 20, pp. 4568–4575, 1980