Degree Type
Honors Capstone Project
Date of Submission
Spring 5-1-2013
Capstone Advisor
Assistant Professor James L. Hougland
Honors Reader
Assistant Professor Heather Coleman
Capstone Major
Biology
Capstone College
Arts and Science
Audio/Visual Component
no
Capstone Prize Winner
no
Won Capstone Funding
yes
Honors Categories
Sciences and Engineering
Subject Categories
Biochemistry | Biochemistry, Biophysics, and Structural Biology
Abstract
Post-translational modifications play an essential role in regulating protein structure and function. Enzymes catalyzing these modifications must often recognize and modify multiple substrate proteins from among a plethora of non-substrates with similar structures and amino acid sequences. For example, protein farnesyltransferase (FTase) catalyzes the addition of an isoprenoid group to a cysteine near the C-terminus of a substrate protein and is proposed to modify a pool of substrates numbering more than one hundred. We seek to understand the interactions in the FTase active site that engender substrate selectivity. By mutating two residues within FTase, we have developed FTase variants with expanded substrate selectivity. The alteration in substrate selectivity observed in our variants suggests that FTase selectivity may depend on a small number of “tunable” active site contacts. Our work provides insight into how this multispecific enzyme recognizes its pool of substrates and will also aid in identifying additional FTase substrates.
Recommended Citation
Zhang, Susan, "Development of Protein Farnesyltransferase Variants with Altered Substrate Selectivity" (2013). Honors Capstone Projects - All. 74.
https://surface.syr.edu/honors_capstone/74
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
