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Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase
The issue of toxins produced by Helicobacter pylori (H. pylori) urgently requires clarification given that the bacterium causes gastric epithelial cell damage which may lead to precancerous and cancerous changes. During an investigation of the possibility of mono(adenosine 5′‐diphosphate (ADP)‐ribos...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
1997
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5921279/ https://www.ncbi.nlm.nih.gov/pubmed/9414650 http://dx.doi.org/10.1111/j.1349-7006.1997.tb00308.x |
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author | Nozaki, Tadashige Masutani, Mitsuko Noda, Takeshi Saito, Daizo Sugiyama, Toshiro Takato, Tsuyoshi Wakabayashi, Keiji Nakagama, Hitoshi Sugimura, Takashi |
author_facet | Nozaki, Tadashige Masutani, Mitsuko Noda, Takeshi Saito, Daizo Sugiyama, Toshiro Takato, Tsuyoshi Wakabayashi, Keiji Nakagama, Hitoshi Sugimura, Takashi |
author_sort | Nozaki, Tadashige |
collection | PubMed |
description | The issue of toxins produced by Helicobacter pylori (H. pylori) urgently requires clarification given that the bacterium causes gastric epithelial cell damage which may lead to precancerous and cancerous changes. During an investigation of the possibility of mono(adenosine 5′‐diphosphate (ADP)‐ribosyl)‐ation by H. pylori products, as observed for other bacterial toxins, we found that radioactivity of [adenylate‐(32)P]nicotinamide adenine dinucleotide (NAD) is incorporated into an H. pylori protein of 80 kDa after incubation with crude bacterial extract. In contrast, [carbonyl‐(14)C]NAD did not show any radioactivity incorporation. Unexpectedly, treatment of the modified protein with 0.1 N HC1, but not 0.1 JV NaOH, released the AMP moiety. Such chemical properties are characteristic of bacterial DNA ligase‐AMP complexes. We found that an antibody raised against Escherichia coli DNA ligase [EC 6.5.1.2] immunoprecipitated the modified 80 kDa protein. Our results indicate that incorporation of radioactivity derived from NAD into the 80 kDa protein was due to adenylation, but not mono‐(ADP‐ribosyl) ation, of the DNA ligase of H. pylori. |
format | Online Article Text |
id | pubmed-5921279 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1997 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-59212792018-05-11 Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase Nozaki, Tadashige Masutani, Mitsuko Noda, Takeshi Saito, Daizo Sugiyama, Toshiro Takato, Tsuyoshi Wakabayashi, Keiji Nakagama, Hitoshi Sugimura, Takashi Jpn J Cancer Res Article The issue of toxins produced by Helicobacter pylori (H. pylori) urgently requires clarification given that the bacterium causes gastric epithelial cell damage which may lead to precancerous and cancerous changes. During an investigation of the possibility of mono(adenosine 5′‐diphosphate (ADP)‐ribosyl)‐ation by H. pylori products, as observed for other bacterial toxins, we found that radioactivity of [adenylate‐(32)P]nicotinamide adenine dinucleotide (NAD) is incorporated into an H. pylori protein of 80 kDa after incubation with crude bacterial extract. In contrast, [carbonyl‐(14)C]NAD did not show any radioactivity incorporation. Unexpectedly, treatment of the modified protein with 0.1 N HC1, but not 0.1 JV NaOH, released the AMP moiety. Such chemical properties are characteristic of bacterial DNA ligase‐AMP complexes. We found that an antibody raised against Escherichia coli DNA ligase [EC 6.5.1.2] immunoprecipitated the modified 80 kDa protein. Our results indicate that incorporation of radioactivity derived from NAD into the 80 kDa protein was due to adenylation, but not mono‐(ADP‐ribosyl) ation, of the DNA ligase of H. pylori. Blackwell Publishing Ltd 1997-10 /pmc/articles/PMC5921279/ /pubmed/9414650 http://dx.doi.org/10.1111/j.1349-7006.1997.tb00308.x Text en |
spellingShingle | Article Nozaki, Tadashige Masutani, Mitsuko Noda, Takeshi Saito, Daizo Sugiyama, Toshiro Takato, Tsuyoshi Wakabayashi, Keiji Nakagama, Hitoshi Sugimura, Takashi Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title | Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title_full | Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title_fullStr | Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title_full_unstemmed | Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title_short | Helicobacter pylori Extracts Exhibit Nicotinamide Adenine Dinucleotide‐derived Adenylation but Not Mono(adenosine 5‐diphosphate‐ribosyOation of DNA Ligase |
title_sort | helicobacter pylori extracts exhibit nicotinamide adenine dinucleotide‐derived adenylation but not mono(adenosine 5‐diphosphate‐ribosyoation of dna ligase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5921279/ https://www.ncbi.nlm.nih.gov/pubmed/9414650 http://dx.doi.org/10.1111/j.1349-7006.1997.tb00308.x |
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