Academic Research Experience

Robert D. Moir, Ph. D.

Dr. Moir’s academic research career covered generally the study of structure of the cell nucleus and the regulation of processes such as DNA replication and transcription that occur within the nucleus. During his career, Dr. Moir gained experience in a wide variety of biochemical, molecular and cell biological techniques. Dr. Moir did his thesis work in the laboratory of Dr. Gordon Dixon at the University of Calgary. The focus of the work in the laboratory was the regulation of gene expression using of the protamine gene family as a model system. Dr. Moir’s thesis work concentrated on a comparison of the protamine gene families from related fish species to identify common DNA regulatory elements involved in gene expression. During the thesis work, Dr. Moir gained expertise in a wide range of techniques in molecular biology including genomic and cDNA library construction and DNA sequencing methods.

For a first postdoctoral fellowship, Dr. Moir went to the Laboratory of Molecular Biology in Cambridge, England to study the nuclear lamin proteins, found in the cell nucleus, with Dr. Murray Stewart. The nuclear lamins have since been linked to human diseases such as progeria, Emery-Dreifuss muscular dystrophy, diabetes and dilated cardiomyopathy. Dr. Moir developed methods to express the human lamin proteins in bacteria. The structural characteristics of the expressed lamin proteins, purified by a series of chromatographic steps, were characterized using high resolution electron microscopy and biochemical assays. The expressed proteins were also assayed for binding to other cellular components such as chromosomes.

Subsequently, Dr. Moir went to Northwestern University Medical School, initially as a postdoctoral fellow and later as research associate professor, to apply cell biological methods to the study of the lamins. The subcellular location of the lamins was characterized using immunofluorescence techniques and by expressing lamin cDNAs fused to the green fluorescent protein in living cells and performing high resolution confocal light microscopy to localize the lamins. In parallel with these experiments, Dr. Moir used the egg extract prepared from Xenopus laevis to study lamin function. The addition of mutant lamin proteins to the egg extract inhibited DNA replication of nuclei assembled in the extract, pointing to a role for the lamins in replication. Dr. Moir also used to this system to examine the role of the lamins in the execution of apoptosis.

Throughout his research career, Dr. Moir has gained experience in a wide range of techniques. These include DNA cloning techniques, including various applications of the polymerase chain reaction. Dr. Moir employed both high resolution electron microcopy and light microscopy to aspects of his lamin research. In addition, he gained a great deal of familiarity with the production and characterization of antibodies and a variety of biochemical methods including those required for protein characterization such as high performance chromatography methods and cell fractionation methods.


Back to Profile	Academic Research Experience Robert D. Moir, Ph. D. Dr. Moir’s academic research career covered generally the study of structure of the cell nucleus and the regulation of processes such as DNA replication and transcription that occur within the nucleus. During his career, Dr. Moir gained experience in a wide variety of biochemical, molecular and cell biological techniques. Dr. Moir did his thesis work in the laboratory of Dr. Gordon Dixon at the University of Calgary. The focus of the work in the laboratory was the regulation of gene expression using of the protamine gene family as a model system. Dr. Moir’s thesis work concentrated on a comparison of the protamine gene families from related fish species to identify common DNA regulatory elements involved in gene expression. During the thesis work, Dr. Moir gained expertise in a wide range of techniques in molecular biology including genomic and cDNA library construction and DNA sequencing methods. For a first postdoctoral fellowship, Dr. Moir went to the Laboratory of Molecular Biology in Cambridge, England to study the nuclear lamin proteins, found in the cell nucleus, with Dr. Murray Stewart. The nuclear lamins have since been linked to human diseases such as progeria, Emery-Dreifuss muscular dystrophy, diabetes and dilated cardiomyopathy. Dr. Moir developed methods to express the human lamin proteins in bacteria. The structural characteristics of the expressed lamin proteins, purified by a series of chromatographic steps, were characterized using high resolution electron microscopy and biochemical assays. The expressed proteins were also assayed for binding to other cellular components such as chromosomes. Subsequently, Dr. Moir went to Northwestern University Medical School, initially as a postdoctoral fellow and later as research associate professor, to apply cell biological methods to the study of the lamins. The subcellular location of the lamins was characterized using immunofluorescence techniques and by expressing lamin cDNAs fused to the green fluorescent protein in living cells and performing high resolution confocal light microscopy to localize the lamins. In parallel with these experiments, Dr. Moir used the egg extract prepared from Xenopus laevis to study lamin function. The addition of mutant lamin proteins to the egg extract inhibited DNA replication of nuclei assembled in the extract, pointing to a role for the lamins in replication. Dr. Moir also used to this system to examine the role of the lamins in the execution of apoptosis. Throughout his research career, Dr. Moir has gained experience in a wide range of techniques. These include DNA cloning techniques, including various applications of the polymerase chain reaction. Dr. Moir employed both high resolution electron microcopy and light microscopy to aspects of his lamin research. In addition, he gained a great deal of familiarity with the production and characterization of antibodies and a variety of biochemical methods including those required for protein characterization such as high performance chromatography methods and cell fractionation methods.