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EXPERIMENTAL PROTOCOLS

Our laboratory team provides help and support with optimization for researchers who would like to use our approach to identify direct RNA-protein interactions. For detailed protocols for RNA antisense purification with mass spectrometry (RAP-MS), please click the links below.

Protocols for UV-crosslinked RNA-protein purification and identification
The most updated version and optimization details for human cancer cells are available in the following article:


Trang N, Su T, Hall S, et al. Streamlined Purification of RNA-Protein Complexes Using UV Cross-Linking and RNA Antisense Purification. Methods Mol Biol. 2023;2666:213-229. doi:10.1007/978-1-0716-3191-1_16
trang_2023_mimb.pdf
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This previous version of RAP-MS is from 2018, and contains details for purification of RNA-protein complexes from mouse embryonic stem cells:

mchugh2018_rap-ms_mimb.pdf
File Size: 384 kb
File Type: pdf
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DIVERSITY AND INCLUSION
Our laboratory team strives to make science approachable, equitable, and inclusive for all who want to participate. We value transparency, data sharing, and open access to scientific findings. Our affiliation with UC San Diego enables our work with a broad range of students and scientists.
Please click for more information about our commitment to advancing equity in education and research: diversity.ucsd.edu

PUBLICATIONS

Su T., Kong L., Cheung D., Zhu J., Chou V., Camden N., Huang C., and McHugh C.A. 2023. GRAS1 non-coding RNA protects against DNA damage and cell death by binding NKAP. bioRxiv 2023.06.20.545783; doi: https://doi.org/10.1101/2023.06.20.545783

Trang N., Su. T., Hall S., Boutros N., Kong B., Huang C. and McHugh, C.A. 2022. Streamlined purification of RNA-protein complexes using UV crosslinking and RNA antisense purification. Methods in Molecular Biology: RNA-Protein Interactions and Complexes (In Press).
 
Burnett C.A., Wong, A.T., Vasquez, C.A., McHugh, C.A., Yeo, G.W., and Komor, A.C. 2022. Examination of the Cell Cycle Dependence of Cytosine and Adenine Base Editors. Frontiers in Genome Editing 4: 932718.

McHugh C.A. and Guttman M. 2018. RAP-MS: A method to identify proteins that interact directly with a specific RNA molecule in cells. In Methods in Molecular Biology: RNA Detection – Methods and Protocols.

McHugh C.A., Chen C.K., Chow A., Surka C.F., Tran C., McDonel P., Pandya-Jones A., Blanco M., Burghard C., Moradian A., Sweredoski M.J., Shishkin A.A., Su J., Lander E.S., Hess S., Plath K., and Guttman M. 2015. The Xist lncRNA interacts directly with SHARP to silence transcription through HDAC3. Nature 521: 232-236.
 
McHugh C.A., Fontana J., Nemecek D., Cheng N., Aksyuk A.A., Heymann J.B., Winkler D.C., Lam A.S., Wall J.S., Steven A.C., and Hoiczyk E. 2014. A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress. EMBO Journal 33: 1896-1911.
 
McHugh C.A., Russell P., and Guttman M. 2014. Methods for comprehensive experimental identification of RNA-protein interactions. Genome Biology 15: 203-212.
 
Koch M.K., McHugh C.A., and Hoiczyk E. 2011. BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape. Molecular Microbiology 80: 1031-1051.
 
Hoiczyk E., Ring M.W., McHugh C.A., Schwär G., Bode E., Krug D., Altmeyer M.O., Lu J.Z., and Bode H.B. 2009. Lipid body formation plays a central role in cell fate determination during developmental differentiation of Myxococcus xanthus. Molecular Microbiology 74: 497-517.
 
Dinglasan R.R., Devenport M., Florens L., Johnson J.R., McHugh C.A., Donnelly-Doman M., Carucci D.J., Yates J.R., and Jacobs-Lorena M. 2009. The Anopheles gambiae adult midgut peritrophic matrix proteome. Insect Biochemistry and Molecular Biology 39: 125-134.
 
Carra J.H., McHugh C.A., Mulligan S., Machiesky L.M., Soares A.S., and Millard C.B. 2007. Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site. BMC Structural Biology 7: 72.
 
Sergueev K., McHugh C.A., and Hoiczyk E. 2006. Type III secretion systems: Bacterial injection devices for microbe-host interactions. In J. M. Shipley (ed), Microbiology Monographs. Vol. 2: Complex intracellular structures in prokaryotes. Springer, Heidelberg; pp. 339-347.
 
McHugh C.A., Tammariello R.F., Millard C.B., and Carra J.H. 2004. Improved stability of a protein vaccine through elimination of a partially unfolded state. Protein Science 13: 2736-43.

TEACHING
Course information for enrolled students is available through UCSD Canvas

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CHEM 109
Recombinant DNA Laboratory
Upper-level Undergraduate

This course introduces students to the tools of molecular biology and how to perform experiments with recombinant DNA techniques.
Prerequisites: CHEM 43A, 143A, 43AM, or 143AM and CHEM 114A.

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 CHEM 164
Structural Biology of Viruses Undergraduate

 An introduction to viral protein and RNA structures and how they facilitate the  viral life cycle from host recognition and entry to replication, assembly, release, and transmission.
Prerequisites: BIBC 100 or CHEM 114A and BIBC 102 or CHEM 114B and BIMM 100 or CHEM 114C

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CHEM 264
Structural Biology of Viruses
Graduate

An introduction to viral protein and RNA structures and how they facilitate the  viral life cycle from host recognition and entry to replication, assembly, release, and transmission. This graduate level course includes a term paper or individual research project.


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