ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1

Sen Zheng, Jun ichi Nagao, Mami Nishie, Takeshi Zendo, Kenji Sonomoto

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)763-772
Number of pages10
JournalApplied Microbiology and Biotechnology
Volume102
Issue number2
DOIs
Publication statusPublished - Jan 1 2018

Fingerprint

Bacteriocins
ATP-Binding Cassette Transporters
Protein Sorting Signals
Adenosine Triphosphatases
Peptide Hydrolases
Nucleotides
Proteins
Staphylococcus
Liposomes
nukacin ISK-1

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1. / Zheng, Sen; Nagao, Jun ichi; Nishie, Mami; Zendo, Takeshi; Sonomoto, Kenji.

In: Applied Microbiology and Biotechnology, Vol. 102, No. 2, 01.01.2018, p. 763-772.

Research output: Contribution to journalArticle

@article{b91c048526cb4fce9b69abba2a6ed635,
title = "ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1",
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.",
author = "Sen Zheng and Nagao, {Jun ichi} and Mami Nishie and Takeshi Zendo and Kenji Sonomoto",
year = "2018",
month = "1",
day = "1",
doi = "10.1007/s00253-017-8645-2",
language = "English",
volume = "102",
pages = "763--772",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer Verlag",
number = "2",

}

TY - JOUR

T1 - ATPase activity regulation by leader peptide processing of ABC transporter maturation and secretion protein, NukT, for lantibiotic nukacin ISK-1

AU - Zheng, Sen

AU - Nagao, Jun ichi

AU - Nishie, Mami

AU - Zendo, Takeshi

AU - Sonomoto, Kenji

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85034665196&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85034665196&partnerID=8YFLogxK

U2 - 10.1007/s00253-017-8645-2

DO - 10.1007/s00253-017-8645-2

M3 - Article

VL - 102

SP - 763

EP - 772

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 2

ER -