1. Volume 20, Issue 1, Pages 111-122 (January 2013)
Heterologous Expression and Engineering Studies of Labyrinthopeptins, Class III Lantibiotics from Actinomadura namibiensis 
Joanna M. Krawczyk, Ginka H. Völler, Bartlomiej Krawczyk, Julian Kretz, Mark Brönstrup, Roderich D. Süssmuth 
Chemistry & Biology 
Volume 20, Issue 1, Pages (January 2013)
DOI: /j.chembiol
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2. Chemistry & Biology 2013 20, 111-122DOI: (10. 1016/j. chembiol. 2012
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3. Figure 1 Structures and Biosynthesis of Labyrinthopeptins
(A) Structures and ring assignments of labyrinthopeptin A1 and A2 (leader peptide sequence given as a one-letter code).
(B) Organization of the labyrinthopeptin (lab) gene cluster with genes coding for the structural genes labA1/A2, the modifying enzyme labKC, and transporters labT1/T2.
(C) Structure of labionin (Lab) and lanthionine (Lan).
(D) Alignment of the core regions of precursor peptides belonging to class III gene clusters with putative ring topologies of labyrinthopeptins (conserved Ser/Ser/Cys motif is highlighted).
Chemistry & Biology  , DOI: ( /j.chembiol )
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4. Figure 2 Expression of Labyrinthopeptin Variants in S. lividans
(A) Vector pUWLab used for expression in Streptomyces hosts.
(B) Detection of the labyrinthopeptin derivatives D-, AD-labyrinthopeptin A1, and NR-labyrinthopeptin A2 from liquid cultures of S. lividans/pUWLab (9d, YEME medium). Total ion chromatogram (TIC, QTrap).
(C) Extracted Ion Chromatogram (EIC, QTrap) over the mass range m/z 1,095.5–1,096.5 corresponding to doubly charged D-labyrinthopeptin A1 and m/z 1,097.5–1,098.5 corresponding to doubly charged NR-labyrinthopeptin A2 (see Table S1). The molecular masses of labyrinthopeptin A1 and A2 were not found in the culture filtrates.
Chemistry & Biology  , DOI: ( /j.chembiol )
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5. Figure 3
Engineering Studies on the Leader Peptide toward Proper Processing by the Proteolytic System of S. lividans
Schematic representations of precursor peptide genes and corresponding product detection by LC-ESI-Orbitrap-MS.
(A) S. lividans/pLab producing AD-, D-labyrinthopeptin A1, and NR-labyrinthopeptin A2.
(B) S. lividans/pLab_SG2 producing labyrinthopeptin A1 and M-labyrinthopeptin A1 (see also Figures S1, S3, and S4).
(C) S. lividans/pLab_SG6 producing AM-, M-, and labyrinthopeptin A2 and ENR-, NR-, and R-labyrinthopeptin A1 (Figures S2 and S3).
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6. Figure 4 Labyrinthopeptin Mutants Expressed in S. lividans
(A) Concept of performed modifications (for cloning strategy, see Figure S5 and Tables S3 and S4).
(B) Overview of Ala exchange mutagenesis performed on LabA1 and LabA2. Observed production levels are represented (gray, >5 mg/l; white, <5 mg/l; white with dotted line, no production).
(C) Overview of prepared mutants (see also Figure S6). Expression of the peptide was evaluated by high-resolving HPLC-MS (detected mutants marked with tick, mutants not detected marked with cross; see Table S2 for observed masses and Figure S7 for MS/MS spectra).
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7. Figure 5
LC-ESI-MS Spectra of In Vitro Conversion of Selected LabA1 Mutants
Comparison of unmodified peptide (upper spectra) and processed peptide (lower spectra). Full processing is represented by the LabA1 peptide and LabA1_N2insA, whereas processing of other peptides results in accumulation of intermediates (indicated masses correspond to most abundant species). See also Figures S8–S10).
Chemistry & Biology  , DOI: ( /j.chembiol )
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