RRC ID |
55092
|
Author |
Zheng S, Nagao JI, Nishie M, Zendo T, Sonomoto K.
|
Title |
ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1.
|
Journal |
Appl Microbiol Biotechnol
|
Abstract |
Lantibiotic nukacin ISK-1 is produced by Staphylococcus warneri ISK-1. The dual functional transporter NukT, an ABC transporter maturation and secretion protein, contributes to cleavage of the leader peptide from the prepeptide (modified NukA) and the final transport of nukacin ISK-1. NukT consists of an N-terminal peptidase domain (PEP), a C-terminal nucleotide-binding domain (NBD), and a transmembrane domain (TMD). In this study, NukT and its peptidase-inactive mutant were expressed, purified, and reconstituted into liposomes for analysis of their peptidase and ATPase activities. The ATPase activity of the NBD region was shown to be required for the peptidase activity of the PEP region. Furthermore, we demonstrated for the first time that leader peptide cleavage by the PEP region significantly enhanced the ATPase activity of the NBD region. Taken together, the presented results offer new insights into the processing mechanism of lantibiotic transporters and the necessity of interdomain cooperation.
|
Volume |
102(2)
|
Pages |
763-772
|
Published |
2018-1-1
|
DOI |
10.1007/s00253-017-8645-2
|
PII |
10.1007/s00253-017-8645-2
|
PMID |
29167920
|
MeSH |
ATP-Binding Cassette Transporters / genetics
ATP-Binding Cassette Transporters / metabolism*
Adenosine Triphosphatases / genetics
Adenosine Triphosphatases / metabolism*
Bacterial Proteins / metabolism
Bacteriocins / biosynthesis*
Biological Transport
Liposomes / metabolism
Membrane Proteins / metabolism
Mutation
Protein Binding
Protein Processing, Post-Translational*
Protein Sorting Signals*
Staphylococcus / genetics
Staphylococcus / metabolism
|
IF |
3.67
|
Times Cited |
5
|
Resource |
General Microbes |
JCM 1157 |