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Elucidation of the Primary Structure of the Lantibiotic Epilancin K7 from Staphylococcus epidermidis K7. Cloning and Characterisation of the Epilancin-K7-Encoding Gene and NMR Analysis of Mature Epilancin K7

1995; Wiley; Volume: 230; Issue: 2 Linguagem: Inglês

10.1111/j.1432-1033.1995.0587h.x

1432-1033

Mart van de Kamp, Henno W. van den Hooven, Ruud N.H. Konings, Gabriele Bierbaum, Hans‐Georg Sahl, Oscar P. Kuipers, Roland J. Siezen, Willem M. de Vos, Cornelis W. Hilbers, F.J.M. van de Ven,

RNA and protein synthesis mechanisms

Lantibiotics are bacteriocins that contain unusual amino acids such as lanthionines and a$-didehydro residues generated by posttranslational modification of a ribosomally synthesized precursor protein.The structural gene encoding the novel lantibiotic epilancin K7 from Staphylococcus epidemzidis K7 was cloned and its nucleotide sequence was determined.The gene, which was named elkA, codes for a 55residue preprotein, consisting of an N-terminal 24-residue leader peptide, and a C-terminal 31 -residue propeptide which is posttranslationally modified and processed to yield mature epilancin K7.In common with the type-A lantibiotics nisin A and nisin Z , subtilin, epidermin, gallidermin and Peps, pre-epilancin K7 has a so-called class-A1 leader peptide.Downstream and upstream of the elk4 gene, the starts of two open-reading-frames, named elkP and elkT, were identified.The elkP and elkT genes presumably encode a leader peptidase and a translocator protein, respectively, which may be involved in the processing and export of epilancin K7.The amino acid sequence of the unmodified pro-epilancin K7, deduced from the elkA gene sequence, is in full agreement with the amino acid sequence of mature epilancin K7, determined previously by means of NMR spectroscopy [van de Kamp, M.,