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Journal of Bacteriology, June 2005, p. 3859-3863, Vol. 187, No. 11
0021-9193/05/$08.00+0     doi:10.1128/JB.187.11.3859-3863.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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

Ekaterina Semenova,1,{dagger} Yulia Yuzenkova,1,{dagger} Jean Peduzzi,2 Sylvie Rebuffat,2 and Konstantin Severinov1*

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.


* Corresponding author. Mailing address: Waksman Institute, 190 Frelinghuysen Road, Piscataway, NJ 08854. Phone: (732) 445-6095. Fax: (732) 445-5735. E-mail: severik{at}waksman.rutgers.edu.

{dagger} These authors contributed equally to this work.


Journal of Bacteriology, June 2005, p. 3859-3863, Vol. 187, No. 11
0021-9193/05/$08.00+0     doi:10.1128/JB.187.11.3859-3863.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




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