Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase.
Peptide microcin J25 (MccJ25) inhibits bacterial RNA polymerase. We show that thermolysin-cleaved MccJ25 and MccJ25 lacking amino acids 13 to 17 also inhibit transcription. Our data and structural analysis of intact and thermolysin-digested MccJ25 suggest that distinct regions of MccJ25 are involved in transcription inhibition and cell entry.
Semenova
Ekaterina
E
Waksman Institute for Microbiology, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, 190 Frelinghuysen Road, Piscataway, New Jersey 08854, USA.
Yuzenkova
Yulia
Y
Peduzzi
Jean
J
Rebuffat
Sylvie
S
Severinov
Konstantin
K
D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000737:chemistry* / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013820:Thermolysin; D014158:Transcription, Genetic
D001430:Bacteriocins; D029968:Escherichia coli Proteins; C020411:microcin; D012321:DNA-Directed RNA Polymerases; D013820:Thermolysin