Professor
Protein Chemistry and Enzymology
E-mail: robert.bateman@usm.edu
Phone: (+1) 601-266-4701, and Fax: 601-266-6075
Website: http://ocean.otr.usm.edu/~w304739/

Education:
1985-88:Post-Doctoral.; Biochemistry; UT Southwestern Medical Center, Dallas, TX
1985: Ph.D.; Biochemistry; University of North Carolina, Chapel Hill, NC
1980: B.S., Biochemistry, Louisiana State University, Baton Rouge, LA

Research interests:

1. Identification and characterization of peptide termini modifying enzymes in humans and other eukaryotes
2. Design, manufacture, and method validation of rapid, solid phase, enzyme-based biosensors for amines released during decomposition or cellular proliferation
3. Identification, purification, and characterization of highly surface active proteins from fish processing byproducts
4. Mechanisms of prebiotic peptide synthesis via thioester intermediates

Research summary:
The primary focus of our research efforts at USM has been the enzymology of biologically active peptides (hormones, neurotransmitters, etc), in particular with the enzyme known as glutaminyl cyclase (QC). QC performs a modification commonly found on many hormones and neurotransmitters which is required for their biological activity and/or stability. With an NIH-FIRST Award our laboratory isolated the DNA sequence coding for the human QC (cDNA), produced the recombinant human protein in bacteria and insect cell culture, and extensively characterized this recombinant protein. We have now done the same with the fruit fly QC and shown that it is nearly identical with the human homolog. Human QC appears to be involved with a number of pathologic states including colon cancer, melanoma, and Alzheimer’s. We hope to better understand the role of QC in these disease states as well as the basic biological and evolutionary relationships between QC and other bioactive peptide processing enzymes. The fold and active site of human QC are shown in the accompanying images. In parallel to the research with animal QC, we have purified and mechanistically characterized

a plant (papaya) QC. The plant QC may be involved in storage of plant seed proteins and possibly also in plant defense mechanisms. A collaboration between our group, a British research group at Leeds and Unizyme (a Danish biotechnology company) led to the isolation of the papaya QC cDNA. The sequence of the plant enzyme proved to be very different from that of its animal counterpart. In fact, there appears to be an entire plant QC family which all differ from animal QC in both sequence and tertiary structure. The plant QC family is now part of our bioinformatics approach to understanding the evolution of peptide processing.

A completely different line of research in our laboratory has developed over the last several years in the area of marine fisheries. This involves a two pronged approach, one in a collaborative project with Dr. Robert Lochhead in Polymer Science to examine protein emulsifiers in processing byproducts of gulf menhaden, and one in a collaborative project with Dr. Margot Hall in Medical Technology to develop biosensors which could be used as a quality control tool to assess seafood spoilage. In the former project we have found that the oily menhaden is rich in protein that goes to the oil-water interface in preference to the air-water interface, a property which is highly desirable in wetting agents. We have received a patent on the use of these agents, and have obtained a modest level of funding from Sea Grant to refine the extraction process. The latter project involved the development of rapid colorimetric sensors or dipsticks which can detect the presence of amines in tissue extracts. We are currently using these dipsticks to test for amines in human urine as potential screens for certain types of cancers.

Recent Publications:

1. Dahl, S.W., Slaughter, C., Lauritzen, C., Bateman, Jr., R.C., Connerton, I. and Pedersen, J. (2000) Carica papaya glutamine cyclotransferase belongs to a novel plant enzyme subfamily, cloning and characterization of the recombinant enzyme. Prot. Exp. Purif.20, 27-36.

2. Word, J.M., Bateman, Jr., R.C., Presley, B., and Richardson, D. (2000) Exploring steric constraints on protein mutations with Mage and Probe. Protein Science 9, 2251-2259.

3. Bateman, Jr., R.C., Temple, J.S., Lovell, S., Booth, R.E. and Misquitta, S.A. (2001) Role of conserved histidines in human pituitary glutaminyl cyclase Biochemistry 40, 11246-11250.

4. Bateman, Jr., R.C., Booth, D., Sirochman, R., Richardson, J., Richardson, D. (2002) Teaching and assessing three-dimensional molecular literacy in undergraduate biochemistry. J. Chem. Ed. 79, 551-552.

5. Bateman, Jr., R.C., (2002) Structure visualization in biochemistry education. J. Miss. Acad. Sci. 47, 149-152.

6. Booth, R.E., Misquitta, S.A and Bateman, Jr., R.C., (2003) Human Pituitary Glutaminyl Cyclase: Expression in Insect Cells and Dye Affinity Purification. Prot. Express Purif. 32, 141-146.

7. Booth, R.E., Lovell S.C., Misquitta, S.A. and Bateman, Jr. R.C. (2004) Human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site BMC Biology 2:2. (10 February 2004) Available at http://www.biomedcentral.com/bmcbiol/

8. Booth, D., Sirochman, R., Richardson, J., Richardson, D. and Bateman, Jr., R.C. (2005) Assessment of Molecular Construction in Undergraduate Biochemistry. J. Chem. Ed. 82, 1854-1858.

9. Stieff, M., Bateman, R., & Uttal, D. (2005). Teaching and learning with three-dimensional representations. In J. K. Gilbert (Ed.), Visualization in science education (pp. 93-120). Oxford: Oxford University Press.

Recent Patents:
Hersh, L.B. and Bateman , Jr., R.C. "Inhibitors of neutral endopeptidase/CALLA as chemotherapeutic agents," issued 4/6/93, US Patent #5,200,426
Lochhead, R., Bateman, Jr., R.C., Tisack, M. and Gololobov, M. “Surfactant properties of menhaden fish protein,” issued 11/16/99, US Patent #5,985,840