Substrate selection by the ClpXP protease : a tail of destruction

(cont.) sites for CIpA and SspB; this spatial arrangement of signals allows for efficient modulation of proteolysis of ssrA-tagged proteins. Finally, additional substrates whose degradation may be regulated by the adaptor protein SspB were determined by identifying substrates captured in ClpXP[trap] in an sspB⁺ strain but not an sspB⁻ strain. This analysis led to the identification of the N-terminal fragment of RseA, the master regulator of the extracytoplasmic stress response, as a protein whose ClpXP-mediated degradation is also enhanced by SspB. Degradation of N-RseA leads to activation of [sigma]E and thus induction of the extra-cytoplasmic stress response. This thesis work has contributed to the understanding of how intracellular proteolysis is regulated to accommodate the selective degradation of a broad range of substrates. ClpXP uses an assortment of recognition strategies, including degradation tags and adaptor proteins, in a combinatorial fashion to regulate protein degradation.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Biology.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2004

Author dc:creator

• Flynn, Julia M., 1976-

Advisor dc:contributor.advisor

• Tania A. Baker.

• Biology.

Statement dc:rights

• 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.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

en_US

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/28679

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/28679