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Proteomic Atomics Reveals a Distinctive Uracil‐5‐Methyltransferase

Title
Proteomic Atomics Reveals a Distinctive Uracil‐5‐Methyltransferase
Author
KUTZNER, ARNE HOLGER
Keywords
Apicoplast; Bioinformatics; Cross species; Malaria; Methyltransferase
Issue Date
2020-01
Publisher
WILEY-V C H VERLAG GMBH
Citation
MOLECULAR INFORMATICS, v.39, no. 5, page. 1-10
Abstract
Carbon (C), hydrogen (H), nitrogen (N), oxygen (O), and sulfur (S) atoms intrigue as they are the foundation for amino acid (AA) composition and the folding and functions of proteins and thus define and control the survival of a cell, the smallest unit of life. Here, we calculated the proteomic atom distribution in >1500 randomly selected species across the entire current phylogenetic tree and identified uracil-5-methyltransferase (U5MTase) of the protozoan parasite Plasmodium falciparum (Pf, strain Pf3D7), with a distinct atom and AA distribution pattern. We determined its apicoplast location and in silico 3D protein structure to refocus attention exclusively on U5MTase with tremendous potential for therapeutic intervention in malaria. Around 300 million clinical cases of malaria occur each year in tropical and subtropical regions of the world, resulting in over one million deaths annually, placing malaria among the most serious infectious diseases. Genomic and proteomic research of the clades of parasites containing Pf is progressing slowly and the functions of most of the similar to 5300 genes are still unknown. We applied a 'bottom-up' comparative proteomic atomics analysis across the phylogenetic tree to visualize a protein molecule on its actual basis - i. e., its atomic level. We identified a protruding Pf3D7-specific U5MTase, determined its 3D protein structure, and identified potential inhibitory drug molecules through in silico drug screening that might serve as possible remedies for the treatment of malaria. Besides, this atomic-based proteome map provides a unique approach for the identification of parasite-specific proteins that could be considered as novel therapeutic targets.
URI
https://onlinelibrary.wiley.com/doi/full/10.1002/minf.201900135https://repository.hanyang.ac.kr/handle/20.500.11754/160134
ISSN
1868-1743; 1868-1751
DOI
10.1002/minf.201900135
Appears in Collections:
COLLEGE OF ENGINEERING[S](공과대학) > INFORMATION SYSTEMS(정보시스템학과) > Articles
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