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Structure-Activity Analysis of Microcin J25: Distinct Parts of the Threaded Lasso Molecule Are Responsible for Interaction with Bacterial RNA Polymerase

Ekaterina Semenova,^1, Yulia Yuzenkova,^1, Jean Peduzzi,² Sylvie Rebuffat,² and Konstantin Severinov^1*

Waksman Institute for Microbiology, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854,¹ Laboratory of Chemistry and Biochemistry of Natural Substances USM 502, UMR 5154 CNRS, Department of Regulations, Development and Molecular Diversity, National Museum of Natural History, Paris, France²

Received 9 November 2004/ Accepted 31 January 2005

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.

These authors contributed equally to this work.