Interaction between two essential, conserved bacterial proteins YeaZ and glycoprotease as a potential antibacterial target in multi-drug-resistant .

Timmie A Britton, Haiyong Guo, Yinduo Ji

Journal: Science progress 2022;103(1):36850419890521

PMID: 31829791

Abstract

Protein-protein interactions among highly conserved and essential proteins can serve as new targets for antibacterial therapies. One protein-protein interaction between two widely conserved and essential bacterial proteins, YeaZ and its paralog, a putative glycoprotease, is being looked into for its antimicrobial drug potential. These two proteins possess tandem functions, including repression of the branched-chain amino acids biosynthesis and induction of a tRNA modification important in enhancing translation fidelity through anticodon-codon base pairing. Heterodimer formation between these two proteins is essential for , and other bacterial species including and . Such YeaZ-glycoprotease interaction could thus be a target for antimicrobial drugs designed for multi-drug-resistant . In this review, we discuss the function, structure, and interaction between these two proteins and their orthologs in other bacteria.

Address: College of Biomedical Science, University of Minnesota, Minneapolis, MN, USA.; College of Life Science, Jilin Normal University, Siping, China.; Department of Veterinary and Biomedical Sciences, College of Veterinary Medicine, University of Minnesota, Minneapolis, MN, USA.
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