Open AccessPlausible Minimal Substrate for Erm Protein
Author(s) -
Hak Jin Lee,
Young In Park,
Hyung Jong Jin
Publication year - 2020
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.00023-20
Subject(s) - firmicutes , actinobacteria , 23s ribosomal rna , lincosamides , escherichia coli , virginiamycin , biology , microbiology and biotechnology , bacteria , bacterial protein , antibiotics , biochemistry , antibiotic resistance , rna , genetics , 16s ribosomal rna , gene , ribosome
Erm proteins methylate a specific adenine residue (A2058, Escherichia coli coordinates) conferring macrolide-lincosamide-streptogramin B (MLS B ) antibiotic resistance on a variety of microorganisms, ranging from antibiotic producers to pathogens. To identify the minimal motif required to be recognized and methylated by the Erm protein, various RNA substrates from 23S rRNA were constructed, and the substrate activity of these constructs was studied using three Erm proteins, namely, ErmB from Firmicutes and ErmE and ErmS from Actinobacteria .