Plausible Minimal Substrate for Erm Protein | Zendy

Hak Jin Lee | Zendy; Young In Park | Zendy; Hyung Jong Jin | Zendy

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Plausible 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 , biology , escherichia coli , 23s ribosomal rna , virginiamycin , microbiology and biotechnology , lincosamides , bacteria , bacterial protein , antibiotics , antibiotic resistance , biochemistry , 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 .

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