Assistant Professor, Center for RNA Molecular Biology (Faculty since 2005) |
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Education: Ph.D.: Biochemistry, University of Wisconsin-Madison, 1999 Postdoc: Howard Hughes Medical Insitute, University of Arizona, 2005 |
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Secondary Appointment in: Department of Molecular Biology |
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Email: jmc71 Office Location: Wood Blgd. W113 Office Phone: 216-368-0299 Office FAX: 216-368-2010 Laboratory Location: W119 Laboratory Phone: 216-368-0276 |
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Gene expression is tightly regulated at each step to ensure accurate communication of instruction from DNA to proteins. To safeguard the fidelity of gene expression, downstream events must be tightly controlled as not to mask the regulatory events that have occurred upstream. For example, repression of mRNA transcription at the DNA level in response to a cue would be irrelevant to overall gene expression if the cytoplasmic pool of transcribed mRNAs were able to be constantly translated. One important and poorly understood step of gene expression, therefore, is cessation of mRNA translation and onset of mRNA degradation.
A majority of mRNA decay initiates by shortening the 3’ polyadenosine tail (deadenylation), followed by 5’ cap cleavage (decapping), and 5’-3’ exonucleolytic digestion. Deadenylation occurs when mRNA is actively translated, however, decapping and exonucleolytic decay are postulated to occur after ribosomes are cleared and in the cytoplasmic structures termed P-bodies. Several correlations support this hypothesis. First, decapping rate is reciprocally proportional to translational initiation rate. Moreover, decapping regulators directly repress translation, and these and additional decay factors and mRNA decay intermediates co-localize in ribosome-free P-bodies. Finally, P-body size and abundance are inversely proportional with mRNA translation and decay status in the cell. Despite these observations, recent findings suggest mRNA degradation may be independent of P-bodies. Specifically, P-body disruption or formation, under certain conditions, is uncoupled from alternations in mRNA translation or mRNA decay. Consequently, an important but unresolved issue is to determine the interplay between translation and mRNA decay and determine the context in which mRNA is degraded. |
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Pubmed Link to Publications
Select Publications Hu, W., Sweet, T., Chamnongpol, S., Baker, K., and Coller, J. (2009) Eukaryotic mRNA decapping occurs on polyribosomes. submitted Sweet, T.J, Boyer, B., Hu, W., Baker, K.E., and Coller, J. (2007) Microtubule disruption stimulates P-body formation. RNA, 13: 493-502. Barbee, S., Estes, P., Cziko, AM., Luedeman, R., Coller, J., Johnson, N., Howlett, I., MacDonald, P., Brand, A., Newbury, S., Levine, R., Wilhelm, J., Nakamura, A., Parker, R., and Ramaswami, R. (2006) Neuronal RNA granules and cytoplasmic processing bodies are similar in composition and function. Neuron, 21:997-1009 Coller J., and Parker R. (2005) General Translational Repression by Activators of mRNA Decapping. Cell 122:875-886. Cheng Z., Coller J., Parker R., and Song H. (2005) Crystal structure of the DEAD box helicase, Dhh1p. RNA 11:1258-1270. Baker K.E.*, Coller J.*, and Parker R. (2004) The yeast Apq12 protein affects nucleocytoplasmic mRNA transport. RNA 10:1352-1358. *Authors contributed equally Coller J., Tucker M., Sheth U., Valencia M., and Parker R. (2001) The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 12:1717-1727. Coller J. (2000) Control of mRNA metabolism via the poly (A) binding protein and development of the tethered function assay. Doctorate Thesis, University of Wisconsin. Gray N., Coller J., Dickson K., and Wickens M. (2000) Multiple portions of poly (A) binding protein stimulate translation in vivo through a poly (A)-independent mechanism. EMBO J 19:4723-4733. Coller J., Gray N., and Wickens M. (1998) mRNA stabilization by poly (A) binding protein is independent of a poly (A) tail and requires translation. Genes & Dev. 12:3226-3235.
REVIEWS AND CHAPTERS Coller, J. and Rueda, D. (2009) RNA research in the Rustbelt. RNA Biol. 6:9-11 Coller J. (2008). Methods to determine mRNA half-life in Saccharomyces cerevisiae Methods Enzymol. 448:267-84. Coller J. and Wickens, M. (2007). Tethered function assays: An adaptable approach to study RNA regulatory proteins Methods Enzymol. 429:299-321 Baker, K.E. and Coller J., (2006) Post-transcriptional control of gene expression: regulating mRNA translation. Genome Biology 7:332. Coller J., and Parker R. (2004) Eukaryotic mRNA decapping. Annu. Rev. Biochem. 73:861-890. Coller J., and Wickens M. (2002) Tethered function assays using 3’UTRs. Methods 26:142-150. |
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