dc.contributor.author | Dickenson, Nicholas E. | |
dc.contributor.author | Picking, William D. | |
dc.date.accessioned | 2019-09-25T18:24:48Z | |
dc.date.available | 2019-09-25T18:24:48Z | |
dc.date.issued | 2012-11-16 | |
dc.identifier | oksd_dickenson_forsterresonanc_2012 | |
dc.identifier.citation | Dickenson, N. E., & Picking, W. D. (2012). Forster resonance energy transfer (FRET) as a tool for dissecting the molecular mechanisms for maturation of the Shigella type III secretion needle tip complex. International Journal of Molecular Sciences, 13(11), 15137-15161. https://doi.org/10.3390/ijms131115137 | |
dc.identifier.uri | https://hdl.handle.net/11244/321454 | |
dc.description.abstract | Forster resonance energy transfer (FRET) provides a powerful tool for monitoring intermolecular interactions and a sensitive technique for studying A-level protein conformational changes. One system that has particularly benefited from the sensitivity and diversity of FRET measurements is the maturation of the Shigella type III secretion apparatus (T3SA) needle tip complex. The Shigella T3SA delivers effector proteins into intestinal cells to promote bacterial invasion and spread. The T3SA is comprised of a basal body that spans the bacterial envelope and a needle with an exposed tip complex that matures in response to environmental stimuli. FRET measurements demonstrated bile salt binding by the nascent needle tip protein IpaD and also mapped resulting structural changes which led to the recruitment of the translocator IpaB. At the needle tip IpaB acts as a sensor for host cell contact but prior to secretion, it is stored as a heterodimeric complex with the chaperone IpgC. FRET analyses showed that chaperone binding to IpaB's N-terminal domain causes a conformational change in the latter. These FRET analyses, with other biophysical methods, have been central to understanding T3SA maturation and will be highlighted, focusing on the details of the FRET measurements and the relevance to this particular system. | |
dc.format | application/pdf | |
dc.language | en_US | |
dc.publisher | MDPI | |
dc.rights | This material has been previously published. In the Oklahoma State University Library's institutional repository this version is made available through the open access principles and the terms of agreement/consent between the author(s) and the publisher. The permission policy on the use, reproduction or distribution of the material falls under fair use for educational, scholarship, and research purposes. Contact Digital Resources and Discovery Services at lib-dls@okstate.edu or 405-744-9161 for further information. | |
dc.title | Forster resonance energy transfer (FRET) as a tool for dissecting the molecular mechanisms for maturation of the Shigella type III secretion needle tip complex | |
osu.filename | oksd_dickenson_forsterresonanc_2012.pdf | |
dc.description.peerreview | Peer reviewed | |
dc.identifier.doi | 10.3390/ijms131115137 | |
dc.description.department | Microbiology and Molecular Genetics | |
dc.type.genre | Article | |
dc.type.material | Text | |
dc.subject.keywords | forster resonance energy transfer (FRET) | |
dc.subject.keywords | type III secretion system | |
dc.subject.keywords | shigella flexneri | |