A novel lantibiotic, nukacin ISK-1, of staphylococcus warneri ISK-1: Cloning of the structural gene and identification of the structure

Toshihiro Sashihara, Hirokazu KimuRa, Toshimasa Higuchi, Asaho Adachi, Hiromi Matsusaki, Kenji Sonomoto, Ayaaki Ishizaki

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Staphylococcus warneri ISK-1, which we had previously reported as Pediococcus sp. ISK-1, produces a novel bacteriocin, nukacin ISK-1. Edman degradation of the chemically reduced nukacin ISK-1 produced a sequence of 27 amino acids, 7 of which were unidentified. Using single-specific-primer-PCR product as a probe, a 3.6-kb HindIII fragment containing the nukacin ISK-1 structural gene (nukA) was cloned and sequenced. The deduced amino acid sequence of nukacin ISK-1 had 57 amino acids, including a 30-amino acid leader region. The propeptide sequence showed significant similarity to those of lacticin-481 type lantibiotics. In the region upstream of nukA, a part of a long open reading frame (ORF), designated as nukM, encoding a putative modification enzyme was oriented in the opposite direction. In the region downstream of nukA, ORF1 was found in which the sequence of the putative translational product was similar to various response regulatory proteins.

Original languageEnglish
Pages (from-to)2420-2428
Number of pages9
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number11
DOIs
Publication statusPublished - Jan 1 2000

Fingerprint

Bacteriocins
Cloning
Staphylococcus
Organism Cloning
Genes
Amino Acids
Amino Acid Sequence
Pediococcus
Open Reading Frames
Degradation
Polymerase Chain Reaction
nukacin ISK-1
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

A novel lantibiotic, nukacin ISK-1, of staphylococcus warneri ISK-1 : Cloning of the structural gene and identification of the structure. / Sashihara, Toshihiro; KimuRa, Hirokazu; Higuchi, Toshimasa; Adachi, Asaho; Matsusaki, Hiromi; Sonomoto, Kenji; Ishizaki, Ayaaki.

In: Bioscience, Biotechnology and Biochemistry, Vol. 64, No. 11, 01.01.2000, p. 2420-2428.

Research output: Contribution to journalArticle

Sashihara, Toshihiro ; KimuRa, Hirokazu ; Higuchi, Toshimasa ; Adachi, Asaho ; Matsusaki, Hiromi ; Sonomoto, Kenji ; Ishizaki, Ayaaki. / A novel lantibiotic, nukacin ISK-1, of staphylococcus warneri ISK-1 : Cloning of the structural gene and identification of the structure. In: Bioscience, Biotechnology and Biochemistry. 2000 ; Vol. 64, No. 11. pp. 2420-2428.
@article{63d19613d02e4031986ecf99abc35b3d,
title = "A novel lantibiotic, nukacin ISK-1, of staphylococcus warneri ISK-1: Cloning of the structural gene and identification of the structure",
abstract = "Staphylococcus warneri ISK-1, which we had previously reported as Pediococcus sp. ISK-1, produces a novel bacteriocin, nukacin ISK-1. Edman degradation of the chemically reduced nukacin ISK-1 produced a sequence of 27 amino acids, 7 of which were unidentified. Using single-specific-primer-PCR product as a probe, a 3.6-kb HindIII fragment containing the nukacin ISK-1 structural gene (nukA) was cloned and sequenced. The deduced amino acid sequence of nukacin ISK-1 had 57 amino acids, including a 30-amino acid leader region. The propeptide sequence showed significant similarity to those of lacticin-481 type lantibiotics. In the region upstream of nukA, a part of a long open reading frame (ORF), designated as nukM, encoding a putative modification enzyme was oriented in the opposite direction. In the region downstream of nukA, ORF1 was found in which the sequence of the putative translational product was similar to various response regulatory proteins.",
author = "Toshihiro Sashihara and Hirokazu KimuRa and Toshimasa Higuchi and Asaho Adachi and Hiromi Matsusaki and Kenji Sonomoto and Ayaaki Ishizaki",
year = "2000",
month = "1",
day = "1",
doi = "10.1271/bbb.64.2420",
language = "English",
volume = "64",
pages = "2420--2428",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "11",

}

TY - JOUR

T1 - A novel lantibiotic, nukacin ISK-1, of staphylococcus warneri ISK-1

T2 - Cloning of the structural gene and identification of the structure

AU - Sashihara, Toshihiro

AU - KimuRa, Hirokazu

AU - Higuchi, Toshimasa

AU - Adachi, Asaho

AU - Matsusaki, Hiromi

AU - Sonomoto, Kenji

AU - Ishizaki, Ayaaki

PY - 2000/1/1

Y1 - 2000/1/1

N2 - Staphylococcus warneri ISK-1, which we had previously reported as Pediococcus sp. ISK-1, produces a novel bacteriocin, nukacin ISK-1. Edman degradation of the chemically reduced nukacin ISK-1 produced a sequence of 27 amino acids, 7 of which were unidentified. Using single-specific-primer-PCR product as a probe, a 3.6-kb HindIII fragment containing the nukacin ISK-1 structural gene (nukA) was cloned and sequenced. The deduced amino acid sequence of nukacin ISK-1 had 57 amino acids, including a 30-amino acid leader region. The propeptide sequence showed significant similarity to those of lacticin-481 type lantibiotics. In the region upstream of nukA, a part of a long open reading frame (ORF), designated as nukM, encoding a putative modification enzyme was oriented in the opposite direction. In the region downstream of nukA, ORF1 was found in which the sequence of the putative translational product was similar to various response regulatory proteins.

AB - Staphylococcus warneri ISK-1, which we had previously reported as Pediococcus sp. ISK-1, produces a novel bacteriocin, nukacin ISK-1. Edman degradation of the chemically reduced nukacin ISK-1 produced a sequence of 27 amino acids, 7 of which were unidentified. Using single-specific-primer-PCR product as a probe, a 3.6-kb HindIII fragment containing the nukacin ISK-1 structural gene (nukA) was cloned and sequenced. The deduced amino acid sequence of nukacin ISK-1 had 57 amino acids, including a 30-amino acid leader region. The propeptide sequence showed significant similarity to those of lacticin-481 type lantibiotics. In the region upstream of nukA, a part of a long open reading frame (ORF), designated as nukM, encoding a putative modification enzyme was oriented in the opposite direction. In the region downstream of nukA, ORF1 was found in which the sequence of the putative translational product was similar to various response regulatory proteins.

UR - http://www.scopus.com/inward/record.url?scp=0034330091&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034330091&partnerID=8YFLogxK

U2 - 10.1271/bbb.64.2420

DO - 10.1271/bbb.64.2420

M3 - Article

C2 - 11193411

AN - SCOPUS:0034330091

VL - 64

SP - 2420

EP - 2428

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 11

ER -