About Dr. Bill Roesler
Ph.D., 1986, University of Saskatchewan, Department of Biochemistry
B.Sc. 1981, High Honours, University of Saskatchewan, Department of Biochemistry
A Brief Biography
Bill Roesler obtained his PhD from the department of Biochemistry, University of Saskatchewan. Following a postdoctoral fellowship in Cleveland, Ohio, he came back to join the department as a faculty member in 1990. In 2011, he became the head of the department. When he’s not teaching, attending meetings, or carrying out experiments on transcription factor regulation, he enjoys the great outdoors through a variety of activities.
Current Research Interests
The nucleus of a mammalian cell contains the 20,000 genes that make up the human genome as well as the enzymes and other machinery that are required their expression. Rather than being simply a “sac” filled with evenly distributed nucleic acid and proteins, the nucleus is composed of a number of different compartments that have specialized functions. One of these, called nuclear speckles, is of particular interest to our lab and is under active investigation. Nuclear speckles, also known as interchromatin granule clusters, reside in areas of the nucleus that are devoid of DNA although often reside adjacent to genes that are activelytranscribed. Nuclear speckles are self-forming bodies, irregular in both shape and size, and are enriched in splicing factors, transcription factors, and 3’-end RNA processing factors. There is accumulating evidence that nuclear speckles act as a reservoir of these factors, from which they are recruited to sites of active transcription or to other compartments in the nucleus where they are needed.
TCERG1 is one such nuclear speckle-enriched protein that our lab is currently focused on. It was initially, characterized as a regulator of transcriptional elongation by RNA polymerase II. Our lab has recently uncovered a second distinct function for protein, that being to inhibit the activity of a transcriptional activator protein, C/EBPa. Interestingly, the inhibitory effect of TCERG1 on C/EBPa requires the relocalization of TCERG1 from nuclear speckles to pericentromeric regions of the genome where C/EBPa resides. Currently, we are identifying and characterizing the domains in bothTCERG1 and in C/EBPa that mediate their interaction and the relocalization event as a means to identifying the mechanism whereby TCERG1 exerts its inhibitory effects.
- Roesler, W.J. and Dreaver-Charles, K. (2018) Responsive eLearning Exercises to Enhance Student Interaction with Metabolic Pathways. Biochemistry. Molec. Biol. Educ., in press. DOI 10.1002/bmb/21112
- Miller, N., Schick, K., Timchenko, N., Harrison, E., and Roesler, W.J. (2016) The Glutamine-Alanine Repeat Domain of TCERG1 is Required for the Inhibition of the Growth Arrest Activity of C/EBPa. J. Cellul. Biochem. 117, 612-620.
- B. Liao, G.A. Hill, and W.J. Roesler, 2012. Stable expression of barley a-amylase in S. cerevisiae for conversion of starch into bioethanol. Biochem Engin J 53, 63-70.
- B. Moazed, S. Banman, G. Wilkinson, and W. Roesler, 2011. TCERG1 inhibits C/EBPa through a mechanism that does not involve sequestration of C/EBPa at pericentromeric heterochromatin. J. Cellul. Biochem 112, 2317-2326
- B. Liao, G.A. Hill, and W.J. Roesler, 2010. Amylolytic activity and fermentative ability of Saccharomyces cerevisiae strains that express barley a-amylase. Biochem Engin J 53, 63-70
- M. Martinez, N. Ichaso, F. Setien, N. Durany, X. Qiu, and W. Roesler, 2010. The D4-desaturation pathway for DHA biosynthesis is operative in the human species. Differences between normal controls and children with the Zellweger syndrome. Lipids Health Dis. 9, 98
- N. Bawa, D. Bear, G. Hill, C. Niu, and W. Roesler, 2010. Fermentation of glucose and starch particles using an inexpensive medium. J. Chem. Technol. Biotechnol. 85, 441-446
- S.L. Banman, P.J. McFie, H.L. Wilson, W.J. Roesler, 2010. Nuclear redistribution of TCERG1 is required for its ability to inhibit the transcriptional and anti-proliferative activities of C/EBPa. J. Cellul. Biochem. 109, 140-151