GLOBAL MAPPING OF PROTEIN-NUCLEIC ACID INTERACTION OF THE RLE LINE R2Bm

Author

Dhamala Santosh

Graduation Semester and Year

2022

Language

English

Document Type

Thesis

Degree Name

Master of Science in Biology

Department

Biology

First Advisor

Shawn Christensen

Abstract

The R2 Long Interspersed Nucleotide Elements (LINEs) is a widely distributed site specific non-LTR retrotransposons that integrates exclusively into host genome’s 28s rRNA genes and replicate by a process called Target Primed Reverse Transcription (TPRT) which is a “copy-out, copy-in” mechanism whereby element protein binds to the mRNA from which they are translated, forming ribonucleic acid protein particles (RNPs). The investigation of nucleic acid-protein interactions using chemical modification of surface amino acid residues on a protein in the presence and absence of nucleic acids is a relatively new application/technique in the field of Mass Spectrometry and particularly significant in studying protein-nucleic acid communication in nucleoprotein complexes. Here we exploit similar technique to modify the lysine surface residues in presence and absence of nucleic acids to gain insights on which lysine residues are involved in DNA/RNA binding. Upon study using selective modification of lysine residues and subsequent mass spectrometry, we find some new residues in R2 protein which are potentially involved in the DNA binding function during retrotransposition.

Keywords

Retrotransposons, Target primed reverse transcription, Protein footprinting, Lysine modification

Disciplines

Biology | Life Sciences

License

This work is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 4.0 International License.

Comments

Degree granted by The University of Texas at Arlington

Recommended Citation

Santosh, Dhamala, "GLOBAL MAPPING OF PROTEIN-NUCLEIC ACID INTERACTION OF THE RLE LINE R2Bm" (2022). Biology Theses. 68.
https://mavmatrix.uta.edu/biology_theses/68