University of Iowa
Department of Biochemistry
4-403 BSB
Iowa City, IA 52242-1109 USA phone: 877-846-8569
or 319-335-7932
fax: (319) 335-9570
biochem@uiowa.edu

Link: iFund

Department of Biochemistry

All Faculty
  • Advances in Oncology -- Fhit Loss in Lung Cancer: Diagnostic and Therapeutic Implications
  • Cell -- Nicotinamide Riboside Promotes Sir2 Silencing and Extends Lifespan via Nrk and Urh1/Pnp1/Meu1 Pathways to NAD+
  • Current Biology -- Crystal Structure of the Worm NitFhit Rosetta Stone Protein Reveals a Nit Tetramer Binding Two Fhit Dimers
  • J Cellurlar Physiology -- The Histidine Triad Superfamily of Nucleotide-Binding Proteins
  • Cell -- Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans
  • Nature Structural Biology -- Crystal Structures of Hint Demonstrate that Histidine Triad Proteins are GalT-related Nucleotide-Binding Proteins
  • Cellular and Molecular Life Sciences -- FHA-RING Ubiquitin Ligases in Cell Division Cycle Control
  • Oncogenomics: Molecular Approaches to Cancer -- Precariously on the Cusp of Oncogenomics
  • Trends in Biochemical Sciences -- NAD+ Metabolism in Health and Disease

Brenner Laboratory

Charles Brenner, Ph.D

The Brenner laboratory conducts research in three project areas.

First, we study the function of histidine triad hydrolases including Hint, Aprataxin, and Fhit, their homologs, and their signaling partners. This work has led us into fascinating areas of biology including sex determination in birds, ataxia-oculomotor apraxia, vitamin C synthesis, and a frequently inactivated proapoptotic tumor suppressor pathway. Going forward, we are focused on the gene expression and epigenetic consequences of loss of Fhit expression in human bronchial epithelial cells.

Second, we are interested in unsolved problems of NAD+ metabolism, especially as related to aging. We recently described two pathways to NAD+ in fungi and humans that originate from nicotinamide riboside, and we are engaged in discovery and validation of additional NAD+ metabolic genes as well. These pathways are of interest because they are regulated by the availability of vitamins and calories. Some of the pathways are induced in response to nerve damage. Thus, though our work is fundamentally based, there is potential for nutritional or therapeutic interventions that could improve human health.

Finally, we are interested in a pathway for translational and post-translational control of the cell cycle at the G1-S and G2-M transitions that we call the Cdc123/D123-Chfr-eIF2gamma axis of cell division control. In this project, we use yeast genetics, enzymology, mass spectrometry and cell biology to identify the targets of RING E3 ubiquiting ligases that are homologous to the Chfr tumor suppressor protein and to identify the ubiquitin conjugating enzymes and other accessory proteins involved in Chf protein target regulation. This interdisciplinary approach has allowed us to establish a dual requirement for Ubc4 and for Ubc13/Mms2 in the cell cycle-delaying activity of yeast Chf2.

For more information on these topics, please download our publications. Please also feel free to contact Brenner lab personnel.

Dr. Brenner's training included yeast genetics with Kunihiro Matsumoto, yeast molecular biology with Tony Brake, enzyme purification and kinetics with Bob Fuller, and X-ray crystallography with Greg Petsko and Dagmar Ringe.

The 2004 book, Oncogenomics: Molecular Approaches to Cancer, is available from Wiley and Amazon. Please read Dr. Franco Cavalli's review of Oncogenomics in the New England Journal of Medicine.

Archival lecture notes are available for courses developed at Jefferson and Dartmouth:

Funded positions are available so please be in touch.

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