Thesis (Ph.D.) - University of St Andrews, January 2007. / Restricted until 30th January 2010.

Thesis (Ph.D.)--University of California, San Francisco, 2004. / Bibliography: leaves 141-150. Also available online.

Thesis (Ph.D.)--Hong Kong University of Science and Technology, 2006. / Includes bibliographical references (leaves 197-228). Also available in electronic version.

Thesis (M.S.)--University of Delaware, 2007. / Principal faculty advisor: Marlene G. Emara, Dept. of Animal & Food Sciences. Includes bibliographical references.

It is well established that cyclin and cyclin-dependent kinase (CDK) form complex that plays a central role in driving cell cycle progression. The fundamental functions of CDK and cyclin are well conserved across eukaryotes. However, gene families encoding the two type of proteins are significantly expanded in multicellular organisms compared with single-cell species. Despite intensive studies on CDK and its associated cyclin in cultured cell lines, especially in cancer cell lines, the partnership between individual CDKs and cyclins remains elusive especially in vivo. Here I present our preliminary results on establishing the molecular function of a well-conserved cyclin L encoded by cyl-1 in C. elegans. Human cyclin L was demonstrated to form a complex with both CDK11 and CDK12, but its association with the latter remains controversial. Despite a possible function in both transcription and pre-mRNA splicing as suggested by in vitro studies or in yeast, the in vivo function of cyclin L has yet been established in any species. To study cyl-1's function in vivo, we generated multiple strains each expressing a chromosomally integrated single-copy transgenes consisting of CYL-1::GFP flanked by its native regulatory sequences using miniMos technique. The transgene demonstrates ubiquitous expression in nuclei across developmental stages and cell types with few exceptions, including maturing oocytes, in which gene activity is known to be shut down, consistent with its function in transcription and splicing. Co-immunoprecipitation followed by mass spectrometry reveals that CYL-1 interacts with both CDK-11 and CDK-12 along with some other uncharacterized factors. Functional validation of these interactions is underway.

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Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2003. / Includes bibliographical references (leaves 127-148). Also available in electronic version. Access restricted to campus users.

published_or_final_version / Anatomy / Doctoral / Doctor of Philosophy