By Clark J.H., Rhodes C.N.
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It might be superfluous to emphasize the significance of digital . spectroscopy in structural or analytic examine. It has now turn into a question of regimen to list the ultra-violet or seen spectra of compounds for reasons of identity or constitution elucidation. The spectrophotonletric tools of research have changed the traditional tools in ever so rnany circumstances.
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As mentioned before, NisB, NisC and their homologues are likely to interact with class IAI leader peptides, whereas an interaction between the large proteins of the CylM family and the class IAII leader peptides was proposed . Leader peptides of the class IAII lantibiotics such as lactococcin DR , salivaricin A, streptococcin A-FF22  and cytolysin  do not contain the -F-N-L-D-V- box typical for class IAI lantibiotics . Unexpectedly, these class IAII leader peptides showed considerable similarities with leaders of the class II non-lantibiotic bacteriocins [21, 40, 146].
PlnB showed highest homology to the histidine protein kinase family and is predicted as an integral protein of the cytoplasmic membrane with six transmembrane domains located in its N-terminus . PlnC and PlnD are very homologous and corresponded to the response regulator family protein of the Staphylococcus aureus agr locus [134, 149, 150]. Additionally, recent findings suggest that two bacteriocins of the two-peptide type (PlnJ and PlnK of the plnJKLR operon and PlnE and PlnF of the plnEFI operon) and a bacteriocin of the one-peptide type (PlnM of the plnMNOP operon) were located adjacent to the plnABCD cluster and could hence be responsible for bacteriocin activity .
Furthermore, they also contained a proteolytic processing site, identical or comparable to the double-glycine cleavage site of class II non-lantibiotic peptides [21, 40, 146]. It is therefore likely that the processing and secretion mechanism of the class IAII lantibiotics more 44 E. Sablon et al. closely resembles that of the non-lantibiotics. In agreement with this model, an ABC transporter including the N-terminal proteolytic domain was encoded in the lactococcin DR (LctT) and cytolysin (CylT) operons, indicating that they share a common mechanism of export with the non-lantibiotic, double-glycine type leader peptide bacteriocins [118, 122].