Construction of Escherichia coli arginine repressor fusion protein and analysis of its function in xer site-specific recombination

Author

• Kholis Abdulrachim, Universiti Malaya

Date of Award

1-1-2000

Thesis Type

Masters

Document Type

Thesis

Divisions

Faculty of Science

Department

Institute of Biological Sciences

Institution

Universiti Malaya

Abstract

In addition to its role in L-arginine biosynthesis in Escherichia coli, arginine repressor (ArgR), the product of the argR gene, also plays an essential role as an obligate accessory protein in Xer site-specific recombination system. A structure-function relationship study of ArgR was performed to understand more about its role in Xcr site-specific recombination. Fusion proteins between ArgRWT (wild-type ArgR) and a biotinylated peptide as well as between ArgRNV (a mutant ArgR) and a biotinylated peptide were constructed. The biotinylated peptide was fused in frame to the amino-tenninus of ArgR WT and ArgRNV, respectively. Xer recombination assays showed that the ArgRWT-biotinylated peptide fusion protein poorly supports cer-mediated recombination in vivo, whereas the ArgRNV-biotinylated peptide fusion protein proficiently supports cer-mediated recombination in vivo. A 30 kDa protein which is the expected size for ArgR WT and ArgRNV-biotinylated peptide fusion protein was succesfully expressed. ArgRNV-biotinylated peptide fusion protein was partially purified.

Initial

snms

Additional Information

Dissertation (M.A) -- Faculty of Science, Universiti Malaya, 2000.

Recommended Citation

Abdulrachim, Kholis, "Construction of Escherichia coli arginine repressor fusion protein and analysis of its function in xer site-specific recombination" (2000). Student Works (2000-2009). 314.
https://knova.um.edu.my/student_works_2000s/314

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.