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You searched for subject:(peptide extension). Showing records 1 – 2 of 2 total matches.

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Duquesne University

1. Henkel, Matthew A. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.

Degree: MS, Biological Sciences, 2009, Duquesne University

P. aeruginosa 1244 (PA1244) possesses an O-linked glycosylation system by which the glycosyltransferase, PilO, transfers a single preassembled O-antigen repeating unit to the C-terminal serine residue of pilin as a posttranslational modification. Previous work has shown that the group II pilin of PA103 can be engineered for glycosylation by extending a C-terminal serine away from the surface with a short stretch of alanine residues (Horzempa et al., 2006a). As an extension of that study, several normally non-glycosylated proteins [PA683 pilin, PA1244 PilA-E. coli (EC) alkaline phosphatase (PhoA) fusion, and EC PhoA] were engineered with C-terminal amino acid extensions and assessed for glycosylation by PilO-mediated glycan modification. Migration patterns on SDS-PAGE and an electrofocusing gel revealed that the TfpY accessory protein does not directly confer a posttranslational modification to group III PA683 pilin. The addition of two C-terminal peptide extensions, an –AAS tripeptide and a 15 amino acid PA1244 derived-peptide tail, to PA683 pilin allowed glycosylation in an LPS polymerization mutant, PA103 wzyPaO11::aacC1, when complemented with PilO. A PA1244 PilA-EC PhoA fusion and EC PhoA engineered with the C-terminal –AAS tripeptide extension were unable to be glycosylated in strain 1244 or PA103 wzyPaO11::aacC1 complemented with PilO. These results suggest the necessity of pilin-specific structures, or the necessity of a membrane anchor for enhancement of PilO substrate recognition. Additionally, larger peptide tail extensions should be considered for testing in future work. Overall, these findings provide further information on glycosylation substrate specificity and suggest the ability to glycosylate normally non-glycosylated proteins in an effort to produce potential conjugate vaccine components. Advisors/Committee Members: Peter A. Castric, Jana Patton-Vogt, Joseph R. McCormick.

Subjects/Keywords: substrate specificity; PilO; peptide extension; Pseudomonas aeruginosa; O-linked glycosylation; vaccine design

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APA (6th Edition):

Henkel, M. A. (2009). Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. (Masters Thesis). Duquesne University. Retrieved from https://dsc.duq.edu/etd/646

Chicago Manual of Style (16th Edition):

Henkel, Matthew A. “Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.” 2009. Masters Thesis, Duquesne University. Accessed January 19, 2020. https://dsc.duq.edu/etd/646.

MLA Handbook (7th Edition):

Henkel, Matthew A. “Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa.” 2009. Web. 19 Jan 2020.

Vancouver:

Henkel MA. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. [Internet] [Masters thesis]. Duquesne University; 2009. [cited 2020 Jan 19]. Available from: https://dsc.duq.edu/etd/646.

Council of Science Editors:

Henkel MA. Evaluation of PilO Substrate Specificity Using Normally Non-Glycosylated Proteins in Pseudomonas Aeruginosa. [Masters Thesis]. Duquesne University; 2009. Available from: https://dsc.duq.edu/etd/646

2. Wu, Cheng. Study of translational control using cell-free translation systems and primer extension inhibition assays.

Degree: PhD, 2008, Oregon Health Sciences University

Subjects/Keywords: Genetic translation; Proteins  – Synthesis; translational control; nascent peptide; ribosome stalling; cell-free translation; primer extension inhibition translational control; nascent peptide; ribosome stalling; cell-free translation; primer extension inhibition translational control; nascent peptide; ribosome stalling; cell-free translation; primer extension inhibition; Peptide Initiation Factors; Protein Biosynthesis

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Wu, C. (2008). Study of translational control using cell-free translation systems and primer extension inhibition assays. (Doctoral Dissertation). Oregon Health Sciences University. Retrieved from doi:10.6083/M4FN1447 ; http://digitalcommons.ohsu.edu/etd/306

Chicago Manual of Style (16th Edition):

Wu, Cheng. “Study of translational control using cell-free translation systems and primer extension inhibition assays.” 2008. Doctoral Dissertation, Oregon Health Sciences University. Accessed January 19, 2020. doi:10.6083/M4FN1447 ; http://digitalcommons.ohsu.edu/etd/306.

MLA Handbook (7th Edition):

Wu, Cheng. “Study of translational control using cell-free translation systems and primer extension inhibition assays.” 2008. Web. 19 Jan 2020.

Vancouver:

Wu C. Study of translational control using cell-free translation systems and primer extension inhibition assays. [Internet] [Doctoral dissertation]. Oregon Health Sciences University; 2008. [cited 2020 Jan 19]. Available from: doi:10.6083/M4FN1447 ; http://digitalcommons.ohsu.edu/etd/306.

Council of Science Editors:

Wu C. Study of translational control using cell-free translation systems and primer extension inhibition assays. [Doctoral Dissertation]. Oregon Health Sciences University; 2008. Available from: doi:10.6083/M4FN1447 ; http://digitalcommons.ohsu.edu/etd/306

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