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Journal of Bacteriology, April 2009, p. 2380-2387, Vol. 191, No. 7
0021-9193/09/$08.00+0 doi:10.1128/JB.00999-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Institute of Molecular Genetics, Russian Academy of Sciences, Moscow 123182, Russia,1 Waksman Institute, Department of Molecular Biology and Biochemistry, Rutgers, the State University, Piscataway, New Jersey 08854,2 Institute of Gene Biology, Russian Academy of Sciences, Moscow 119991, Russia,3 Rega Institute for Medical Research, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium,4 Institute of Organic Chemistry, Russian Academy of Sciences, Moscow 119991, Russia,5 Department of Chemistry, Moscow State University, Moscow 119991, Russia,6 Central Research Institute of Chemistry and Mechanics, Moscow 115487, Russia,7 Engelhardt Institute of Molecular Biology of Russian Academy of Sciences, Moscow 119991, Russia8
Received 20 July 2008/ Accepted 8 January 2009
Microcin C (McC), an inhibitor of the growth of enteric bacteria, consists of a heptapeptide with a modified AMP residue attached to the backbone of the C-terminal aspartate through an N-acyl phosphamidate bond. Here we identify maturation intermediates produced by cells lacking individual mcc McC biosynthesis genes. We show that the products of the mccD and mccE genes are required for attachment of a 3-aminopropyl group to the phosphate of McC and that this group increases the potency of inhibition of the McC target, aspartyl-tRNA synthetase.
Published ahead of print on 23 January 2009.
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