Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans

Wendy A. Woodruff, Jan Novak, Page W. Caufield

Research output: Contribution to journalArticle

Abstract

Streptococcus mutans, along with many other Gram-positive bacteria produce small antibacterial peptides called bacteriocins. Bacteriocins elaborated by S. mutans, termed mutacins, may provide a selective force necessary for initial or sustained colonization in dental plaque by this major dental pathogen. Previously, we purified and characterized mutacin II, the first lantibiotic found in S. mutans. Specific oligonucleotides designed according to the N-terminal amino acid sequence permitted amplification of 0.7 kb upstream and 2.1 kb downstream of the N-terminus, using single-specific-primer PCR (SSP-PCR). The gene encoding the mutacin II prepeptide, mutA, was subsequently cloned and sequenced. The complete prepeptide consists of 53 amino acids, including the 26 amino acid amphipathic leader peptide with the Gly-2-Gly-1 sequence at the processing site. The prepeptide showed similarity to the lantibiotics lacticin 481, variacin, salivaricin and streptococcin A-FF22. A 3 kb open reading frame immediately downstream of mutA, denoted mutM, showed sequence similarities to LCNDR2 from Lactococcus lactis. By analogy, mutM is probably involved in post-translational modification of the mutacin prepeptide. Gene disruption with an insertional vector pVA891 showed that intact copies of mutA and mutM are required for production of mutacin II.

Original languageEnglish (US)
Pages (from-to)37-43
Number of pages7
JournalGene
Volume206
Issue number1
DOIs
StatePublished - Jan 5 1998

Fingerprint

Bacteriocins
Streptococcus mutans
Sequence Analysis
Genes
Amino Acids
Dental Plaque
Lactococcus lactis
Gram-Positive Bacteria
Post Translational Protein Processing
Protein Sorting Signals
Oligonucleotides
Open Reading Frames
Amino Acid Sequence
Tooth
Polymerase Chain Reaction
Peptides
mutacin II
A-FF22

Keywords

  • Antimicrobial peptide
  • Bacteriocin
  • Nucleotide sequence
  • Post-translational modification

ASJC Scopus subject areas

  • Genetics

Cite this

Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans. / Woodruff, Wendy A.; Novak, Jan; Caufield, Page W.

In: Gene, Vol. 206, No. 1, 05.01.1998, p. 37-43.

Research output: Contribution to journalArticle

Woodruff, Wendy A. ; Novak, Jan ; Caufield, Page W. / Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans. In: Gene. 1998 ; Vol. 206, No. 1. pp. 37-43.
@article{085586c4ea2e4b9289558a22deeeabc2,
title = "Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans",
abstract = "Streptococcus mutans, along with many other Gram-positive bacteria produce small antibacterial peptides called bacteriocins. Bacteriocins elaborated by S. mutans, termed mutacins, may provide a selective force necessary for initial or sustained colonization in dental plaque by this major dental pathogen. Previously, we purified and characterized mutacin II, the first lantibiotic found in S. mutans. Specific oligonucleotides designed according to the N-terminal amino acid sequence permitted amplification of 0.7 kb upstream and 2.1 kb downstream of the N-terminus, using single-specific-primer PCR (SSP-PCR). The gene encoding the mutacin II prepeptide, mutA, was subsequently cloned and sequenced. The complete prepeptide consists of 53 amino acids, including the 26 amino acid amphipathic leader peptide with the Gly-2-Gly-1 sequence at the processing site. The prepeptide showed similarity to the lantibiotics lacticin 481, variacin, salivaricin and streptococcin A-FF22. A 3 kb open reading frame immediately downstream of mutA, denoted mutM, showed sequence similarities to LCNDR2 from Lactococcus lactis. By analogy, mutM is probably involved in post-translational modification of the mutacin prepeptide. Gene disruption with an insertional vector pVA891 showed that intact copies of mutA and mutM are required for production of mutacin II.",
keywords = "Antimicrobial peptide, Bacteriocin, Nucleotide sequence, Post-translational modification",
author = "Woodruff, {Wendy A.} and Jan Novak and Caufield, {Page W.}",
year = "1998",
month = "1",
day = "5",
doi = "10.1016/S0378-1119(97)00578-7",
language = "English (US)",
volume = "206",
pages = "37--43",
journal = "Gene",
issn = "0378-1119",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Sequence analysis of mutA and mutM genes involved in the biosynthesis of the lantibiotic mutacin II in Streptococcus mutans

AU - Woodruff, Wendy A.

AU - Novak, Jan

AU - Caufield, Page W.

PY - 1998/1/5

Y1 - 1998/1/5

N2 - Streptococcus mutans, along with many other Gram-positive bacteria produce small antibacterial peptides called bacteriocins. Bacteriocins elaborated by S. mutans, termed mutacins, may provide a selective force necessary for initial or sustained colonization in dental plaque by this major dental pathogen. Previously, we purified and characterized mutacin II, the first lantibiotic found in S. mutans. Specific oligonucleotides designed according to the N-terminal amino acid sequence permitted amplification of 0.7 kb upstream and 2.1 kb downstream of the N-terminus, using single-specific-primer PCR (SSP-PCR). The gene encoding the mutacin II prepeptide, mutA, was subsequently cloned and sequenced. The complete prepeptide consists of 53 amino acids, including the 26 amino acid amphipathic leader peptide with the Gly-2-Gly-1 sequence at the processing site. The prepeptide showed similarity to the lantibiotics lacticin 481, variacin, salivaricin and streptococcin A-FF22. A 3 kb open reading frame immediately downstream of mutA, denoted mutM, showed sequence similarities to LCNDR2 from Lactococcus lactis. By analogy, mutM is probably involved in post-translational modification of the mutacin prepeptide. Gene disruption with an insertional vector pVA891 showed that intact copies of mutA and mutM are required for production of mutacin II.

AB - Streptococcus mutans, along with many other Gram-positive bacteria produce small antibacterial peptides called bacteriocins. Bacteriocins elaborated by S. mutans, termed mutacins, may provide a selective force necessary for initial or sustained colonization in dental plaque by this major dental pathogen. Previously, we purified and characterized mutacin II, the first lantibiotic found in S. mutans. Specific oligonucleotides designed according to the N-terminal amino acid sequence permitted amplification of 0.7 kb upstream and 2.1 kb downstream of the N-terminus, using single-specific-primer PCR (SSP-PCR). The gene encoding the mutacin II prepeptide, mutA, was subsequently cloned and sequenced. The complete prepeptide consists of 53 amino acids, including the 26 amino acid amphipathic leader peptide with the Gly-2-Gly-1 sequence at the processing site. The prepeptide showed similarity to the lantibiotics lacticin 481, variacin, salivaricin and streptococcin A-FF22. A 3 kb open reading frame immediately downstream of mutA, denoted mutM, showed sequence similarities to LCNDR2 from Lactococcus lactis. By analogy, mutM is probably involved in post-translational modification of the mutacin prepeptide. Gene disruption with an insertional vector pVA891 showed that intact copies of mutA and mutM are required for production of mutacin II.

KW - Antimicrobial peptide

KW - Bacteriocin

KW - Nucleotide sequence

KW - Post-translational modification

UR - http://www.scopus.com/inward/record.url?scp=0032484693&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032484693&partnerID=8YFLogxK

U2 - 10.1016/S0378-1119(97)00578-7

DO - 10.1016/S0378-1119(97)00578-7

M3 - Article

VL - 206

SP - 37

EP - 43

JO - Gene

JF - Gene

SN - 0378-1119

IS - 1

ER -