Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.

Vesicles, specialized cell structures thought to be the site of nitrogen fixation in the actinorhizal bacteria, were isolated from Frankia sp. strain EAN1pec by using French pressure disruption of mycelia followed by differential and isopycnic gradient centrifugation. The isolated vesicles reduced a...

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Main Authors: Tisa, L S, Ensign, J C
Formato: Artigo
Idioma:en
Publicado em: 1987
Assuntos:
Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC213907/
https://ncbi.nlm.nih.gov/pubmed/3478333
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spelling pubmed-2139072003-12-01 Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec. Tisa, L S Ensign, J C J Bacteriol Research Article Vesicles, specialized cell structures thought to be the site of nitrogen fixation in the actinorhizal bacteria, were isolated from Frankia sp. strain EAN1pec by using French pressure disruption of mycelia followed by differential and isopycnic gradient centrifugation. The isolated vesicles reduced acetylene when incubated anaerobically with Mg2+ ions, ATP, and dithionite. No nitrogenase activity was detected in the disrupted mycelial fractions. Vesicles permeabilized by freeze-thaw or detergents showed increased rates of acetylene reduction due to increased permeability of dithionite. The effect on nitrogenase activity of different ATP concentrations was the same in normal and permeabilized vesicles. The endogenous respiratory rate of vesicles was significantly lower than that of mycelia, and the respiration rate of vesicles did not increase following the addition of succinate. The low respiratory activity of vesicles and their apparent dependence on externally supplied ATP for acetylene reduction suggest that the energy and reducing power for nitrogen fixation may be supplied from the mycelia to which they are attached. 1987-11 /pmc/articles/PMC213907/ /pubmed/3478333 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Tisa, L S
Ensign, J C
Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
description Vesicles, specialized cell structures thought to be the site of nitrogen fixation in the actinorhizal bacteria, were isolated from Frankia sp. strain EAN1pec by using French pressure disruption of mycelia followed by differential and isopycnic gradient centrifugation. The isolated vesicles reduced acetylene when incubated anaerobically with Mg2+ ions, ATP, and dithionite. No nitrogenase activity was detected in the disrupted mycelial fractions. Vesicles permeabilized by freeze-thaw or detergents showed increased rates of acetylene reduction due to increased permeability of dithionite. The effect on nitrogenase activity of different ATP concentrations was the same in normal and permeabilized vesicles. The endogenous respiratory rate of vesicles was significantly lower than that of mycelia, and the respiration rate of vesicles did not increase following the addition of succinate. The low respiratory activity of vesicles and their apparent dependence on externally supplied ATP for acetylene reduction suggest that the energy and reducing power for nitrogen fixation may be supplied from the mycelia to which they are attached.
author Tisa, L S
Ensign, J C
author_facet Tisa, L S
Ensign, J C
author_sort Tisa, L S
title Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
title_short Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
title_full Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
title_fullStr Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
title_full_unstemmed Isolation and nitrogenase activity of vesicles from Frankia sp. strain EAN1pec.
title_sort isolation and nitrogenase activity of vesicles from frankia sp. strain ean1pec.
publishDate 1987
url https://ncbi.nlm.nih.gov/pmc/articles/PMC213907/
https://ncbi.nlm.nih.gov/pubmed/3478333
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