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Updated: Aug 11, 2026

Fluorescence Based Primer Extension Technique to Determine Transcriptional Starting Points and Cleavage Sites of RNases In Vivo
Published on: October 31, 2014
Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for
Ekaterina Semenova1, Yulia Yuzenkova, Jean Peduzzi
1Waksman Institute for Microbiology, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, 190 Frelinghuysen Road, Piscataway, New Jersey 08854, USA.
Abstract:
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.
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