Effects of secondary structure of the leader peptide on modification and processing of bovicin HJ50

Abstract:

Abstract:［Objective］ Elucidating the correlation between the secondary structure of the leader peptide of lantibiotic bovicin HJ50 and its modification and processing．［Methods］The variants with mutated leader peptide were synthesized by semi-in vitro biosynthesis，and their modification pattern were then analyzed by MALDI-TOF MS．At the same time，the effect of leader peptide mutants on processing the modified propeptide was examined by HPLC and antimicrobial activity．［Results］ We constructed 6 mutants (F-16A，V-15E，E-14L，E-8P，L-7D，L-4K) involved in forming secondary structure of the bovicin HJ50 leader peptide． F-16A，V-15E，L-4K showed very little effect on modification and processing whereas E-14L and E-8P caused changes in modification． In addition，we found that L-7D strongly affected the processing．［Conclusion］The conserved helix structure in the leader peptide of bovicin HJ50 was closely related to the activity of BovM and BovT150，and the presence of secondary structure was very important to modification and processing of bovicin HJ50．

Key words:Keywords: lantibiotics，leader peptide，modification and processing，site-directed mutagenesis，secondary structure