scholarly journals The killer protein Gasdermin D

2016 ◽  
Vol 23 (12) ◽  
pp. 1897-1898 ◽  
Author(s):  
John A Wright ◽  
Clare E Bryant
Keyword(s):  
Killer Protein

Killer toxin of Pichia membranifaciens and its possible use as a biocontrol agent against grey mould disease of grapevine

Microbiology ◽  
2004 ◽  
Vol 150 (8) ◽  
pp. 2527-2534 ◽  
Author(s):  
A. Santos ◽  
D. Marquina
Keyword(s):  
Killer Toxin ◽  
Grey Mould ◽  
Toxin Production ◽  
Killer Activity ◽  
Pichia Membranifaciens ◽  
Sds Page ◽  
Toxin Protein ◽  
Killing Action ◽  
Killer Protein ◽  
Potential Use

The use of Pichia membranifaciens CYC 1106 killer toxin against Botrytis cinerea was investigated. This strain exerted a broad-specificity killing action against other yeasts and fungi. At pH 4, optimal killer activity was observed at temperatures up to 20 °C. At 25 °C the toxic effect was reduced to 70 %. The killer activity was higher in acidic medium. Above about pH 4·5 activity decreased sharply and was barely noticeable at pH 6. The killer toxin protein from P. membranifaciens CYC 1106 was purified to electrophoretic homogeneity. SDS-PAGE of the purified killer protein indicated an apparent molecular mass of 18 kDa. Killer toxin production was stimulated in the presence of non-ionic detergents. The toxin concentrations present in the supernatant during optimal production conditions exerted a fungicidal effect on a strain of B. cinerea. The symptoms of infection and grey mould observed in Vitis vinifera plants treated with B. cinerea were prevented in the presence of purified P. membranifaciens killer toxin. The results obtained suggest that P. membranifaciens CYC 1106 killer toxin is of potential use in the biocontrol of B. cinerea.

The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: induction of DNA cleavage and blocking of transcription 1 1J. Karn

1997 ◽  
Vol 273 (4) ◽  
pp. 826-839 ◽  
Author(s):  
Susan E Critchlow ◽  
Mary H O’Dea ◽  
Alison J Howells ◽  
Martine Couturier ◽  
Martin Gellert ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Dna Gyrase ◽  
F Plasmid ◽  
Killer Protein

scholarly journals Computational approach and functional analysis of the Pectobacterium carotovorum subsp. carotovorum low-molecular weight bacteriocin Carocin S2

2020 ◽  
Author(s):  
Jyun-Wei Wang ◽  
Ruchi Briam James S. Lagitnay ◽  
Reymund C. Derilo ◽  
Jian-Li Wu ◽  
Duen-Yau Chuang
Keyword(s):  
Cell Attachment ◽  
Coiled Coil ◽  
Site Directed Mutagenesis ◽  
Structural Function ◽  
Pectobacterium Carotovorum ◽  
Immunity Protein ◽  
Bioinformatic Tools ◽  
Carotovorum Subsp ◽  
Killer Protein

AbstractPectobacterium carotovorum subsp. Carotovorum 3F3 is a gram-negative phyto-parasitic enterobacterium. This strain is a producer of Carocin S2 bacteriocin, which comprises of two proteins of different sizes. Carocin S2K (killer protein) which is responsible for antibiotic resistance and Carocin S2I (immunity protein) which inhibits the antibiotic activity.The present study aimed to predict the structure and functional properties of Carocin S2. Computational approaches utilizing various bioinformatic tools predicted that Carocin S2 is a putative membrane protein having the N-terminal at the extracellular side and the central domain at the coiled-coil region. Carocin S2 was predicted to have three domains, the translocation domains, receptor binding domain and the killer domain. Moreover, the killer domain was calculated to have the catalytic cleft. The in-vivo assays confirmed that for Carocin S2K, bound immunity protein was not a pre-requisite for cell attachment or translocation. The site-directed mutagenesis experiment led us to hypothesized the hydrolysis mechanism of Carocin S2.The predicted structure of Carocin S2K provided a system of understanding on the biochemical and structural function which led to the mechanism of Carocin S2. It revealed that the role of immunity protein to Carocin S2 is not a pre-requisite for translocation pathway. Furthermore, this research led to hypothesized a hydrolytic mechanism of Carocin S2 to target the tRNA.

scholarly journals Identification and Characterization of the Bacteriocin Carocin S3 from the Multiple Bacteriocin Producing Strain of Pectobacterium Carotovorum Subsp. Carotovorum

2020 ◽  
Author(s):  
REYMUND CALLANGA DERILO ◽  
Jyun-Wei Wang ◽  
Ruchi Briam James Lagitnay ◽  
Huang-Pin Wu ◽  
Kai-In Chen ◽  
...  
Keyword(s):  
Soft Rot ◽  
Nuclease Activity ◽  
Antimicrobial Activities ◽  
Indicator Strain ◽  
Open Reading Frames ◽  
Economic Losses ◽  
Pectobacterium Carotovorum ◽  
High Concentration ◽  
The Many ◽  
Killer Protein

Abstract BackgroundPectobacterium carotovorum subsp. carotovorum belongs to the Enterobacteriaceae family which causes soft rot disease in numerous plants worldwide resulting in significant economic losses. Results from our previous studies showed that the strain H-rif-8-6 produces low-molecular-weight bacteriocin (LMWB) Carocin S1. Interestingly, TH22-10, the caroS1K:Tn5 insertional mutant in H-rif-8-6, loses Carocin S1 producing ability, but still produces other LMWBs which can be detected by using the indicator strain SP33. The SP33 is one of the many strains that are sensitive toward the cytotoxic effects of CaroS3K, but not Carocin S1. The result revealed that H-rif-8-6 is a multiple-bacteriocin producing strain.ResultsIn this study, a 4.1-kb DNA fragment was isolated by a DNA probe using the caroS1K gene as the template. DNA sequencing and analysis by GenBank revealed two complete open reading frames (ORFs), designated ORF1 and ORF2, which were identified within the sequence fragment. ORF1 and ORF2, similar to the identified Carocin S2 genes, encode the killer (CaroS3K) and the immunity (CaroS3I) proteins, respectively, which were homologous to the colicin E3 gene. CaroS3K and CaroS3I were expressed, isolated, and purified in Escherichia coli BL21 after subcloning of the expression plasmid pGS3KI or pGSK3I. SDS-PAGE analysis showed that the relative masses of CaroS3K and CaroS3I were 95 kDa and 10 kDa, respectively. The results reveal that CaroS3K has higher antimicrobial and specific antimicrobial activities for Pcc along with a nuclease activity than CaroS3I. However, CaroS3I inhibits the activity of CaroS3K. Interestingly, high concentration of CaroS3I protein is also a DNA nuclease, and its activity is also inhibited by CaroS3K.ConclusionThis study showed that another type of bacteriocin was found in Pectobacterium carotovorum. This new type of bacteriocin, Carocin S3, has the killer protein, CaroS3K, and the immunity protein, CaroS3I.

scholarly journals Purification, Circular Dichroism Analysis, Crystallization and Preliminary X-ray Diffraction Analysis of the F Plasmid CcdB Killer Protein

1993 ◽  
Vol 231 (2) ◽  
pp. 513-515 ◽  
Author(s):  
Jan Steyaert ◽  
Laurence Van Melderen ◽  
Phillipe Bernard ◽  
Minh Hoa Dao Thi ◽  
Remy Loris ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Diffraction Analysis ◽  
X Ray Diffraction ◽  
F Plasmid ◽  
X Ray ◽  
Circular Dichroism Analysis ◽  
Killer Protein ◽  
Circular Dichroïsm

scholarly journals Type a Bax Channels: The Highly Voltage-Gated Form of this Killer Protein

2013 ◽  
Vol 104 (2) ◽  
pp. 660a
Author(s):  
Shang H. Lin ◽  
Meenu N. Perera ◽  
Toan Nguyen ◽  
Marco Colombini
Keyword(s):  
Type A ◽  
Voltage Gated ◽  
Killer Protein

Genes & cells: Cellular assassin's surprise benefit: Disabling killer protein might encourage repeated cancers

Science News ◽  
2010 ◽  
Vol 178 (5) ◽  
pp. 8-8
Author(s):  
Tina Hesman Saey
Keyword(s):  
Killer Protein

scholarly journals KILLER PHENOMENON IN USTILAGO MAYDIS: THE ORGANIZATION OF THE VIRAL GENOME

Genetics ◽  
1978 ◽  
Vol 88 (2) ◽  
pp. 267-276
Author(s):  
Y Koltin ◽  
J S Kandel
Keyword(s):  
Viral Genome ◽  
Ustilago Maydis ◽  
Double Stranded Rna ◽  
Virus Like Particles ◽  
Killer Strain ◽  
Additional Support ◽  
Killer Protein ◽  
Coding Capacity

ABSTRACT The double-stranded RNA content, the production of inactive killer protein, and the presence of virus-like particles were examined in induced nonkiller mutants and nonkiller progeny from a cross between a killer strain and a sensitive strain. A correlation between the loss of the 0.7 × 106 daltons dsRNA of the Ustilago maydis P6 virus and the lack of synthesis of the killer protein was established. In vitro and in vivo complementation between nonkiller strains provide additional support for the suggestion that the 0.7 × 106 daltons dsRNA is related to the killer function. The coding capacity of the various species of dsRNA is discussed in relation to their possible function.

scholarly journals Identification and Characterization of the Bacteriocin Carocin S3 from the Multiple Bacteriocin Producing Strain of Pectobacterium carotovorum subsp. carotovorum

2020 ◽  
Author(s):  
Jyun-Wei Wang ◽  
Reymund Callanga Derilo ◽  
Ruchi Briam James Lagitnay ◽  
Huang-Pin Wu ◽  
Kai-In Chen ◽  
...  
Keyword(s):  
Soft Rot ◽  
Nuclease Activity ◽  
Antimicrobial Activities ◽  
Indicator Strain ◽  
Open Reading Frames ◽  
Economic Losses ◽  
Pectobacterium Carotovorum ◽  
Chromosomal Dna ◽  
High Concentration ◽  
Killer Protein

Abstract Background: Pectobacterium carotovorum subsp. carotovorum belongs to the Enterobacteriaceae family, which causes soft-rot disease in numerous plants worldwide resulting in significant economic losses. Results from our previous studies showed that the strain H-rif-8-6 produces low-molecular-weight bacteriocin (LMWB) Carocin S1. Interestingly, TH22-10, the caroS1K:Tn5 insertional mutant in H-rif-8-6, loses Carocin S1 producing ability, but still produces other LMWBs which the indicator strain SP33 can detect. The SP33 is one of the many strains that are sensitive toward the cytotoxic effects of Carocin S3K, but not Carocin S1. The result revealed that H-rif-8-6 is a multiple-bacteriocin producing strain.Results: In this study, a 4.1-kb DNA fragment was isolated from the chromosomal DNA of Pcc strain, H-rif-8-6, by a DNA probe using the caroS1K gene as the template. DNA sequencing and analysis by GenBank revealed two complete open reading frames (ORFs), designated ORF1 and ORF2, which were identified within the sequence fragment. ORF1 and ORF2, similar to the identified carocin S2 genes, encode the killer (Carocin S3K) and the immunity (Carocin S3I) proteins, respectively, which were homologous to the colicin E3 gene. Carocin S3K and Carocin S3I were expressed, isolated, and purified in Escherichia coli BL21 after subcloning of the expression plasmid pGS3KI or pGSK3I. SDS-PAGE analysis showed that the relative masses of Carocin S3K and Carocin S3I were 95.6 kDa and 10.2 kDa, respectively. The results reveal that Carocin S3K has higher antimicrobial and specific antimicrobial activities for Pcc along with a nuclease activity than Carocin S3I. However, Carocin S3I inhibits the activity of Carocin S3K. Interestingly, a high concentration of Carocin S3I protein is also a DNA nuclease, and Carocin S3K also inhibits its activity.Conclusion: This study showed that another type of bacteriocin was found in Pectobacterium carotovorum. This new type of bacteriocin, Carocin S3, has the killer protein, Carocin S3K, and the immunity protein, Carocin S3I.

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