A Novel Deoxyribonuclease Low-Molecular-Weight Bacteriocin, Carocin S4, from Pectobacterium carotovorum subsp. carotovorum

Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional...

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Published inMicroorganisms (Basel) Vol. 11; no. 7; p. 1854
Main Authors Wu, Huang-Pin, Derilo, Reymund C., Hsu, Shih-Hao, Hu, Jia-Ming, Chuang, Duen-Yau
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 22.07.2023
MDPI
Subjects
bacteriocin
Bacteriocins
calcium
Calcium ions
Carocin
Cloning
Deoxyribonuclease
deoxyribonucleases
Deoxyribonucleic acid
divalent metals
DNA
E coli
Functional analysis
genes
Genomics
Homology
immunity
immunity protein
killer protein
low-molecular-weight bacteriocin
Magnesium
Metal ions
mutants
Nuclease
Open reading frames
Pectobacterium carotovorum
Pectobacterium carovotorum subsp. carotovorum
Plasmids
Proteins
Ribonuclease
ribonucleases
Rifampin
temperature
Temperature requirements
Zinc
United States > US
Japan
immunity protein
Pectobacterium carovotorum subsp. carotovorum
killer protein
bacteriocin
low-molecular-weight bacteriocin
Carocin
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Abstract Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg2+, Ca2+, and Zn2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
AbstractList Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg2+, Ca2+, and Zn2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg2+, Ca2+, and Zn2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
Pectobacterium carotovorum subsp . carotovorum ( Pcc ) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc . A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc . CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg 2+ , Ca 2+ , and Zn 2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc , with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg2+, Ca2+, and Zn2+ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from Pcc. A 2750 bp gene fragment was isolated from the chromosomal DNA of Pcc mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains caroS4K and caroS4I within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from Pcc. CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg²⁺, Ca²⁺, and Zn²⁺ to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in Pcc, with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
subsp ( ) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by several factors. In this paper, we report the discovery, isolation, characterization, and functional analysis of Carocin S4, a novel low-molecular-weight bacteriocin (LMWB) from . A 2750 bp gene fragment was isolated from the chromosomal DNA of mutant strain rif-TO6, a rifampicin-resistant strain of TO6. The gene contains and within two open reading frames, which encode CaroS4K and CaroS4I, with molecular weights of about 90 kD and 10 kD, respectively. The unique characteristics of Carocin S4 were revealed after homology analysis with the previously discovered bacteriocins from . CaroS4K, which shares 23% and 85% homology with CaroS1K and CaroS3K, respectively, is also a deoxyribonuclease. However, unlike the two which can only hydrolyze genomic DNA, CaroS4K hydrolyzes both genomic and plasmid DNA. On the other hand, CaroS4K was found to be 90% homologous with CaroS2K but works differently in killing the target cell, as the latter is a ribonuclease. The optimal reaction temperature for CaroS4K to hydrolyze dsDNA is approximately 50 °C and requires the divalent metal ions Mg , Ca , and Zn to catalyze its DNase activity. This study reveals another nuclease type of bacteriocin in , with CaroS4K and CaroS4I functioning as killer and immunity proteins, respectively.
Author Derilo, Reymund C.
Hu, Jia-Ming
Wu, Huang-Pin
Hsu, Shih-Hao
Chuang, Duen-Yau
AuthorAffiliation 4 College of Teacher Education, Nueva Vizcaya State University-Bambang Campus, Bambang 3702, Philippines
2 College of Medicine, Chang Gung University, Taoyuan 33302, Taiwan
1 Division of Pulmonary, Critical Care and Sleep Medicine, Chang Gung Memorial Hospital, Keelung 33305, Taiwan; whanpyng@cgmh.org.tw
3 Department of Chemistry, National Chung-Hsing University, Taichung City 40227, Taiwan; rcderilo@nvsu.edu.ph (R.C.D.); shinhaohsu@gmail.com (S.-H.H.); jamyhu2010@gmail.com (J.-M.H.)
AuthorAffiliation_xml – name: 2 College of Medicine, Chang Gung University, Taoyuan 33302, Taiwan
– name: 3 Department of Chemistry, National Chung-Hsing University, Taichung City 40227, Taiwan; rcderilo@nvsu.edu.ph (R.C.D.); shinhaohsu@gmail.com (S.-H.H.); jamyhu2010@gmail.com (J.-M.H.)
– name: 1 Division of Pulmonary, Critical Care and Sleep Medicine, Chang Gung Memorial Hospital, Keelung 33305, Taiwan; whanpyng@cgmh.org.tw
– name: 4 College of Teacher Education, Nueva Vizcaya State University-Bambang Campus, Bambang 3702, Philippines
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  orcidid: 0000-0001-5416-2353
  surname: Derilo
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/37513026$$D View this record in MEDLINE/PubMed
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CitedBy_id crossref_primary_10_1016_j_rhisph_2024_100908
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Issue 7
Keywords immunity protein
Pectobacterium carovotorum subsp. carotovorum
killer protein
bacteriocin
low-molecular-weight bacteriocin
Carocin
Language English
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These authors contributed equally to this work.
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Snippet Pectobacterium carotovorum subsp. carotovorum (Pcc) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related...
subsp ( ) is known to produce different types of bacteriocins, active protein substances that inhibit or kill related strains and are known to be induced by...
Pectobacterium carotovorum subsp . carotovorum ( Pcc ) is known to produce different types of bacteriocins, active protein substances that inhibit or kill...
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StartPage 1854
SubjectTerms bacteriocin
Bacteriocins
calcium
Calcium ions
Carocin
Cloning
Deoxyribonuclease
deoxyribonucleases
Deoxyribonucleic acid
divalent metals
DNA
E coli
Functional analysis
genes
Genomics
Homology
immunity
immunity protein
killer protein
low-molecular-weight bacteriocin
Magnesium
Metal ions
mutants
Nuclease
Open reading frames
Pectobacterium carotovorum
Pectobacterium carovotorum subsp. carotovorum
Plasmids
Proteins
Ribonuclease
ribonucleases
Rifampin
temperature
Temperature requirements
Zinc
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Title A Novel Deoxyribonuclease Low-Molecular-Weight Bacteriocin, Carocin S4, from Pectobacterium carotovorum subsp. carotovorum
URI https://www.ncbi.nlm.nih.gov/pubmed/37513026
https://www.proquest.com/docview/2843083730
https://www.proquest.com/docview/2844084913
https://www.proquest.com/docview/3040353375
https://pubmed.ncbi.nlm.nih.gov/PMC10386115
https://doaj.org/article/9e13c2877f0d4a9cb13636f26f4e5199
Volume 11
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