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Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72

Thomas Hurek, Marc Van Montagu UGent, Eduard Kellenberger and Barbara Reinhold-Hurek (1995) MOLECULAR MICROBIOLOGY. 18(2). p.225-236
abstract
We report the discovery of novel subcellular structures related to bacterial nitrogen fixation in the strictly respiratory diazotrophic bacterium Azoarcus sp, BH72, which was isolated as an endophyte from Kallar grass, Nitrogenase is derepressed under microaerobic conditions at O-2 concentrations in the micromolar range. With increasing O-2 deprivation, bacteria can develop into a hyperinduced state, which is characterized by high specific rates of respiration and efficient nitrogen fixation at approximately 30 nM O-2 Ultrastructural analysis of cells in the course of hyperinduction revealed that complex intracytoplasmic membrane systems are formed, which consist of stacks of membranes and which are absent under standard nitrogen-fixing conditions, The iron protein of nitrogenase was highly enriched on these membranes, as evidenced by immunohistochemical studies, Membrane deficiency in NifH/K- mutants, a deletion mutant in the nifK gene and the character of NH4+-grown cells suggested, in concert with the membrane localization of nitrogenase, that these structures are specialized membranes related to nitrogen fixation. We propose the term 'diazosomes' for them, Development of intracytoplasmic membranes coincides with the appearance of a high-molecular-mass form of the iron protein of nitrogenase, which was detectable in membrane fractions, Mutational analysis, and determination of the N-terminal amino acid sequence indicate that the nifH gene product is covalently modified by a mechanism probably different from adenosine diphosphoribosylation. Development of diazosomes in nitrogen-fixing cells can be induced in pure cultures and in co-culture with a fungus isolated from the rhizosphere of Kallar grass.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ELECTROPHORESIS, AZOSPIRILLUM, IRON PROTEIN, DIAZOTROPHIC RODS, RHIZOBIUM-MELILOTI, RHODOSPIRILLUM-RUBRUM, KALLAR GRASS, GENE-EXPRESSION, AZOTOBACTER-VINELANDII, ESCHERICHIA-COLI
journal title
MOLECULAR MICROBIOLOGY
Mol. Microbiol.
volume
18
issue
2
pages
225 - 236
Web of Science type
Article
ISSN
0950-382X
DOI
10.1111/j.1365-2958.1995.mmi_18020225.x
language
English
UGent publication?
yes
classification
A1
additional info
correction published in Mol. Microbiol. (1996) 21(6), 1299
copyright statement
I have transferred the copyright for this publication to the publisher
id
196139
handle
http://hdl.handle.net/1854/LU-196139
date created
2004-01-14 13:42:00
date last changed
2013-11-06 13:41:35
@article{196139,
  abstract     = {We report the discovery of novel subcellular structures related to bacterial nitrogen fixation in the strictly respiratory diazotrophic bacterium Azoarcus sp, BH72, which was isolated as an endophyte from Kallar grass, Nitrogenase is derepressed under microaerobic conditions at O-2 concentrations in the micromolar range. With increasing O-2 deprivation, bacteria can develop into a hyperinduced state, which is characterized by high specific rates of respiration and efficient nitrogen fixation at approximately 30 nM O-2 Ultrastructural analysis of cells in the course of hyperinduction revealed that complex intracytoplasmic membrane systems are formed, which consist of stacks of membranes and which are absent under standard nitrogen-fixing conditions, The iron protein of nitrogenase was highly enriched on these membranes, as evidenced by immunohistochemical studies, Membrane deficiency in NifH/K- mutants, a deletion mutant in the nifK gene and the character of NH4+-grown cells suggested, in concert with the membrane localization of nitrogenase, that these structures are specialized membranes related to nitrogen fixation. We propose the term 'diazosomes' for them, Development of intracytoplasmic membranes coincides with the appearance of a high-molecular-mass form of the iron protein of nitrogenase, which was detectable in membrane fractions, Mutational analysis, and determination of the N-terminal amino acid sequence indicate that the nifH gene product is covalently modified by a mechanism probably different from adenosine diphosphoribosylation. Development of diazosomes in nitrogen-fixing cells can be induced in pure cultures and in co-culture with a fungus isolated from the rhizosphere of Kallar grass.},
  author       = {Hurek, Thomas and Van Montagu, Marc and Kellenberger, Eduard and Reinhold-Hurek, Barbara},
  issn         = {0950-382X},
  journal      = {MOLECULAR MICROBIOLOGY},
  keyword      = {ELECTROPHORESIS,AZOSPIRILLUM,IRON PROTEIN,DIAZOTROPHIC RODS,RHIZOBIUM-MELILOTI,RHODOSPIRILLUM-RUBRUM,KALLAR GRASS,GENE-EXPRESSION,AZOTOBACTER-VINELANDII,ESCHERICHIA-COLI},
  language     = {eng},
  number       = {2},
  pages        = {225--236},
  title        = {Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.1995.mmi\_18020225.x},
  volume       = {18},
  year         = {1995},
}

Chicago
Hurek, Thomas, Marc Van Montagu, Eduard Kellenberger, and Barbara Reinhold-Hurek. 1995. “Induction of Complex Intracytoplasmic Membranes Related to Nitrogen Fixation in Azoarcus Sp. BH72.” Molecular Microbiology 18 (2): 225–236.
APA
Hurek, T., Van Montagu, M., Kellenberger, E., & Reinhold-Hurek, B. (1995). Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72. MOLECULAR MICROBIOLOGY, 18(2), 225–236.
Vancouver
1.
Hurek T, Van Montagu M, Kellenberger E, Reinhold-Hurek B. Induction of complex intracytoplasmic membranes related to nitrogen fixation in Azoarcus sp. BH72. MOLECULAR MICROBIOLOGY. 1995;18(2):225–36.
MLA
Hurek, Thomas, Marc Van Montagu, Eduard Kellenberger, et al. “Induction of Complex Intracytoplasmic Membranes Related to Nitrogen Fixation in Azoarcus Sp. BH72.” MOLECULAR MICROBIOLOGY 18.2 (1995): 225–236. Print.