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Title:Dissection of Connective Beta -Strand Linkers and Their Role in Enzymatic Activities of Escherichia Coli Leucyl -Trna Synthetase
Author(s):Mascarenhas, Anjali Paulette
Doctoral Committee Chair(s):Martinis, Susan A.
Department / Program:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Chemistry, Biochemistry
Abstract:Individual glycine residues, when mutated to proline, misaminoacylate tRNALeu in spite of retaining efficient amino acid editing activities. It is possible that these mutant LeuRSs may have impaired the translocation of editing substrates between the aminoacylation and editing active sites. An additional T252A mutation within the editing active site in the CP1 was combined with the translocation mutants and these double mutant LeuRSs were characterized in vitro and in vivo. The T252A mutant hydrolyzes both cognate and noncognate amino acids charged to tRNALeu, thereby significantly reducing the yield of charged tRNA. However, beta-strand-based mutants rescue leucylation activity of the T252A mutant LeuRS, suggesting an important role in the translocation pathway. Taken together, this investigation implies a more extensive role for the dynamic beta-strands at different steps of E. coli LeuRS enzyme activity.
Issue Date:2008
Description:163 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008.
Other Identifier(s):(MiAaPQ)AAI3314848
Date Available in IDEALS:2015-09-25
Date Deposited:2008

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