The discriminator domain : does it reside at the C-terminus or the N-terminus of Escherichia coli Lon? Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/qr46r3767

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  • The mechanisms of substrate recognition by regulatory proteases are not well understood. Presently, two opposing models have arisen to describe E. coil Lon's ability to discriminate between substrates: one suggests the N-terminus involvement while the second suggests the C-terminus involvement. In this project, the role of the C-terminal domain as it relates to the recognition of Lon's normal physiological substrates RcsA, an activator of colanic acid capsular polysaccharide, and SulA, an inhibitor of cell division, was addressed. Using site-directed mutagenesis, five mutations in Lon (R537G, E538A, GS40W, R542G, R542P) were isolated. Their phenotypic impact was either similar in character to wildtype Lon (R537G, E538A) or Δlon cells (G540W, R542G, R542P). The stabilization of both RcsA and SulA based on phenotypic assays and immunological detection of lon* strains (G540W, R542G, R542P) suggests the C-terminal domain may be involved in substrate degradation as opposed to discriminator activity.
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  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-08-10T16:59:53Z (GMT) No. of bitstreams: 1 MillerDarceyL2002.pdf: 2483578 bytes, checksum: f8b989b0509da6ab876d27620f4bd23e (MD5)
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