Mechanism and specificity of bacterial two-component signaling systems
Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Biology, 2010.
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| Format: | Thesis |
| Language: | eng |
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Massachusetts Institute of Technology
2010
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| Online Access: | http://hdl.handle.net/1721.1/57799 |
| _version_ | 1826210707299893248 |
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| author | Lubin, Emma A. (Emma Alexandra) |
| author2 | Michael T. Laub. |
| author_facet | Michael T. Laub. Lubin, Emma A. (Emma Alexandra) |
| author_sort | Lubin, Emma A. (Emma Alexandra) |
| collection | MIT |
| description | Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Biology, 2010. |
| first_indexed | 2024-09-23T14:53:53Z |
| format | Thesis |
| id | mit-1721.1/57799 |
| institution | Massachusetts Institute of Technology |
| language | eng |
| last_indexed | 2024-09-23T14:53:53Z |
| publishDate | 2010 |
| publisher | Massachusetts Institute of Technology |
| record_format | dspace |
| spelling | mit-1721.1/577992019-04-13T00:05:59Z Mechanism and specificity of bacterial two-component signaling systems Lubin, Emma A. (Emma Alexandra) Michael T. Laub. Massachusetts Institute of Technology. Dept. of Biology. Massachusetts Institute of Technology. Dept. of Biology. Biology. Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Biology, 2010. Includes bibliographical references (p. 57-60). Bacterial two component signaling (TCS) systems are the predominant means by which bacteria sense and respond to external signals. These systems represent a large family of paralogous proteins; often hundreds of the histidine kinase (HK) and response regulator (RR) pairs that make up a TCS system can be found in a single cell. How do these systems maintain faithful signal transmission and avoid cross-talk? To understand how specificity is determined, we examined co-evolving residues between HKs and RRs, and guided by this, aimed to rewire specificity of several activities of TCS systems. Previous work in the lab has successfully rewired specificity of histidine kinases for response regulators in the phosphotransfer reaction. By mutating different subsets of these co-evolving residues, we were able to rewire specificity of RRs in the phosphotransfer reaction, and partially rewire specificity of HKs and RRs in the phosphatase reaction. Additionally, we identified residues that may dictate specificity between two domains of the histidine kinase, and found that mutating them altered the rate of autophosphorylation. These analyses will allow rational rewiring of two component systems in vivo, and permit us to examine the fitness consequences of this altered specificity, providing insight into the evolutionary pressures on TCS systems. by Emma A. Lubin. S.M. 2010-08-31T14:48:45Z 2010-08-31T14:48:45Z 2010 2010 Thesis http://hdl.handle.net/1721.1/57799 654432839 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 68 p. application/pdf Massachusetts Institute of Technology |
| spellingShingle | Biology. Lubin, Emma A. (Emma Alexandra) Mechanism and specificity of bacterial two-component signaling systems |
| title | Mechanism and specificity of bacterial two-component signaling systems |
| title_full | Mechanism and specificity of bacterial two-component signaling systems |
| title_fullStr | Mechanism and specificity of bacterial two-component signaling systems |
| title_full_unstemmed | Mechanism and specificity of bacterial two-component signaling systems |
| title_short | Mechanism and specificity of bacterial two-component signaling systems |
| title_sort | mechanism and specificity of bacterial two component signaling systems |
| topic | Biology. |
| url | http://hdl.handle.net/1721.1/57799 |
| work_keys_str_mv | AT lubinemmaaemmaalexandra mechanismandspecificityofbacterialtwocomponentsignalingsystems |