Citation

Jin HJ. Korean Journal of Microbiology 2008; 44(3): 193-198.

Copyright

(Copyright © 2008)

DOI

unavailable

PMID

unavailable

Abstract

ErmSF is one of the proteins which are produced by Streptomyces fradiae to avoid suicide by its autogenous macrolide antibiotic, tylosin and one of ERM proteins which are responsible for transferring the methyl group to A2058 (Escherichia coli coordinate) in 23S rRNA, which reduces the affinity of MLS (macrolide-lincosamide-streptogramin B) antibiotics to 23S rRNA, thereby confers the antibiotic resistance on microorganisms ranging from antibiotic producers to pathogens. ErmSF contains an extra N-terminal end region (NTER), which is unique to ErmSF and 25% of amino acids of which is arginine known well to interact with RNA. Noticeably, arginine is concentrated in 58RARR61 and functional role of each arginine in this motif was investigated through deletion and site-directed mutagenesis and the activity of mutant proteins in cell. R60 and R61 was found to play an important role in enzyme activity through the study with deletion mutant up to R60 and R61. With the site-directed mutagenesis using deletion mutant of 1 to 59 (R60A, R61A, and RR60,61AA), R60 was found more important than R61 but R61 was necessary for the proper activity of R60 and vice versa. And these amino acids were presumed to assume a secondary structure of α-helix. Copyright © 2008, The Microbiological Society of Korea.

Language: ko

Keywords

Escherichia coli; Deletion mutagenesis; Growth curve; In vivo activity; Leaky expression; Overexpression; Site-directed mutagenesis MLSB (macrolide-lincosamide-streptogramin B) antibiotic resistance factor protein; Streptomyces fradiae