ErmSF N-말단 부위와 기질인 23S rRNA domain V 중 stem 73-75와의 상호작용 연구 = Studies on Interactions of ErmSF N-terminal End Region with Substrate, stem 73-75 of 23S rRNA domain V

다국어 초록 (Multilingual Abstract)

Microorganisms including pathogens predominantly exhibit the resistance to the MLS (macrolide-lincosamide-streptogramin B) antibiotics by dimethylation of the single adenine residue of 23S rRNA. This chemical modification is mediated by a group of enzymes named erm proteins. One of Erm protein ErmSF, from Streptmyces fradiae, recognizes motifs within domain V of the rRNA that specifically targets adenine 2085 (A2085 in Bacillus subtilis numbering) for methylation. Unlike the other homologous proteins, ErmSF contains long N-terminal end region (63 amino acids) and it contains 25% arginine residues (15/63 amino acids). To find out the interaction mode between N-terminal end region and substrate 23S rRNA, we cloned the DNA fragment coding N-terminal end region polypeptide that NTER(N-terminal end region)1-49, 1-39 and 26-71 by PCR, overexpressed, purified. Using the EMSA(electrophoretic gel mobility shift assay) analysis, we demonstrated that NTER1-49 and NTER1-39 specific interact with the stem 73 and the NTER 26-71 peptides specific interact with the part of stem 75 of 23S rRNA domain V.