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Plausible Minimal Substrate for Erm Protein.

Hak Jin Lee1,2, Young In Park3, Hyung Jong Jin4

  • 1Department of Life Science, Korea University Graduate School, Seoul, Republic of Korea.

Antimicrobial Agents and Chemotherapy
|June 24, 2020
PubMed
Summary

Researchers identified the minimal RNA motif (15 nucleotides) recognized by ErmS for methylation, conferring macrolide-lincosamide-streptogramin B (MLSB) antibiotic resistance. This finding aids understanding Erm protein mechanisms.

Keywords:
Erm proteinantibiotic resistancemethylationminimal substrate

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Area of Science:

  • Molecular Biology
  • Microbiology
  • Biochemistry

Background:

  • Erm proteins methylate adenine at position 2058 in 23S rRNA, conferring resistance to macrolide-lincosamide-streptogramin B (MLSB) antibiotics.
  • This resistance mechanism is found in diverse microorganisms, including pathogens and antibiotic producers.

Purpose of the Study:

  • To determine the minimal RNA motif required for recognition and methylation by Erm proteins.
  • To investigate substrate recognition and methylation mechanisms of ErmB, ErmE, and ErmS proteins.

Main Methods:

  • Construction and analysis of various 23S rRNA-derived RNA substrates.
  • Enzymatic assays using three Erm proteins (ErmB, ErmE, ErmS) to assess methylation activity.

Main Results:

  • The shortest identified substrate motif is 15 nucleotides, recognized and methylated by ErmS.
  • This minimal motif includes A2051 to A2058 and its complementary strand, mimicking a structural feature of 23S rRNA.
  • Protein-specific differences in methylation, cooperativity, and allostery were observed among Erm proteins.

Conclusions:

  • The minimal RNA motif for ErmS methylation is defined, providing insights into Erm protein-RNA interactions.
  • Understanding these minimal substrate requirements can elucidate the binding, recognition, and methylation mechanisms of Erm proteins.
  • Further structural studies of protein-RNA complexes are needed to fully reveal the methylation process.