The prlC Suppressor Phenotype and Its Relation to Oligopeptidase a Specificity
Flores, Theresa M.
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https://hdl.handle.net/2142/86629
Description
Title
The prlC Suppressor Phenotype and Its Relation to Oligopeptidase a Specificity
Author(s)
Flores, Theresa M.
Issue Date
2001
Doctoral Committee Chair(s)
Miller, Charles G.
Department of Study
Microbiology
Discipline
Microbiology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
Abstract
Comparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.
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