The research interests of our faculty span a broad spectrum of biochemistry ranging from cell and developmental biology to structural biology. The unifying theme defining us is an interest in biological processes at the molecular level. The department is home to state of the art facilities and instruments for X-ray crystallography, NMR spectroscopy, mass spectrometry, fluorescence microscopy, to name just a few. A collaborative and collegial atmosphere makes the Biochemistry Department an ideal place to do science and train for a wide variety of biomedical science careers.
Dr. Richard Sabina was elected Vice-Chair of the Association of Biochemistry Course Directors (ABCD) and will begin a 2 year term as Chair in 2011.
The Association of Biochemistry Course Directors (ABCD), founded in 2008, represents course directors and faculty with teaching responsibilities in undergraduate medical courses with a major biochemistry, molecular biology, genetics and/or nutrition component from medical schools in North America, including the 50 United States and Puerto Rico, Canada, Mexico and the Caribbean. The ABCD is concerned with issues related to biomedical education in North American medical schools, such as course and curricular organization, integration of clinical applications into the basic science years and basic science into the clinical years, design of effective small group exercises, creation of effective case-based exam questions, active learning in the large lecture format and training the future generation of medical science educators. The ABCD is also committed to proactively planning for upcoming curricular challenges, such as medical school expansion and the changing format of the USMLE board exams.
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Mailing Address: Medical College of Wisconsin Department of Biochemistry BSB - 3rd Floor 8701 Watertown Plank Road Milwaukee, WI 53226
Gene Reader structurally defined—MCW scientists in the Department of Biochemistry have recently defined the three-dimensional structure (see the figure) of the protein machine that reads the genetic information of genes from eukaryotic cells like those of humans. This protein is called RNA polymerase II and is comprised of a dozen of smaller proteins (or subunits) that assemble into a gigantic apparatus. The polymerase reads through tracks of DNA like a locomotive and, in doing so, produces polymeric RNA molecules in a process known as transcription. The RNA transcripts will go on to cause proteins to be made by the cell. Peter Meyer and colleagues from Dr. Fu laboratory applied an X-ray crystallographic approach to accurately determine the entire protein structure, and their studies have revealed several elements that are crucial to the function of the polymerase. (For a more detailed description, see the webpage of Fu lab. This research has been funded by the NIH and American Cancer Society.)
Brandon T. Larsen MD, PhD and Christopher R. Henry MD
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Dr. Brian Volkman, Associate Professor, and Davin Jensen, Research Technologist III, Coauthors of "Abscisic Acid Inhibits Type 2 C Protein Phosphatases Via the PYR/PYL Family of ABA-Binding START Proteins" published in Science.
Dr. Volkman's laboratory contributed to the study by monitoring the binding of a plant hormone to its receptor using the MCW biomolecular nuclear magnetic resonance (NMR) facility. Davin Jensen produced isotope-labeled samples of the PYR1 protein and performed two- dimensional NMR experiments on the 600 MHz NMR instrument. By comparing the patterns of NMR signals for the protein before and after adding ABA to the sample they saw changes that proved that the hormone binds directly to PYR1, confirming its biological function as the abscisic acid receptor. Another set of NMR experiments showed that PYR1 can interact with another protein, an enzyme called HAB1, but that this interaction only occurs when the hormone is present.
The corresponding author of the study, Dr. Sean Cutler (University of California at Riverside), identified the PYR1 protein in a chemical genomic screen designed to identify receptors for ABA, a hormone of intense interest to plant biologists since its discovery in 1963. ABA regulates many aspects of plant growth and development, and participates in adaptive responses to environmental stress, but its mode of action has remained unknown for over 40 years. The plant biology field has experienced recent disappointments when high-profile reports of the discovery of an ABA receptor were subsequently retracted because other groups were unable to confirm the result. As a consequence, Dr. Cutler anticipated that multiple lines of experimental evidence would be required to convince skeptical experts.
By searching online databases related to protein structure, he learned that Dr. Volkman's research group had previously solved the 3D structure of another plant protein (called MLP28) that may be very similar to PYR1. To strengthen the argument that PYR1 is indeed an ABA receptor protein, Dr. Cutler contacted Dr. Volkman for help confirming the hormone-receptor interaction using NMR spectroscopy, a key tool for structural biology research. By validating his discovery with a combination of genetic, biochemical and structural evidence, including NMR data, Dr. Cutler and his collaborators have opened a new chapter in plant biology.
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Mary L Holtz, PhD and Ravi P Misra, PhD have a paper that has been published in BMC Developmental Biology. Read More.
Dumrongkiet Arthan in the Park lab. Josh Ziarek in the Volkman lab. Josh Weiner in the Volkman lab.
More about our Summer Research Students.