Identification of a second site compensatory mutation in the Fe‐protein that allows diazotrophic growth of <i>Azotobacter vinelandii</i> UW97

Shi, Lei; Pulakat, Lakshmi; Suh, Man-Hee; Gavini, Nara

doi:10.1016/s0014-5793(00)01847-0

Cited by 3 publications

(2 citation statements)

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“…The switch I region in the Fe protein communicates between the nucleotide‐binding site and the docking interface, and previous mutagenesis studies has suggested that residues 59 to 67 are important protein–protein docking interactions 42. In addition, substitution of Av2 Lys170, which has been implicated in interacting with Av1 Glu residues (Table III), gave rise to an inactive Fe protein 43…”

Section: Resultsmentioning

confidence: 99%

The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus

Sen

Peters

2005

Proteins

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The nitrogenase Fe protein is a key component of the biochemical machinery responsible for the process of biological nitrogen fixation. The Fe protein is a member of a class of nucleotide-binding proteins that couple the binding and hydrolysis of nucleoside triphosphates to conformational changes. The nucleotide-dependent conformational changes modulate the formation of a macromolecular complex, and some members of the class include Galpha, EF-Tu, and myosin. The members of this class are highly interesting model systems for the analysis of aspects of thermal adaptability, since their mechanisms involve protein conformational change and protein-protein interactions. In this study, we have used our extensive knowledge of the structure of the Azotobacter vinelandii nitrogenase Fe protein in multiple structural conformations, and standard homology modeling approaches have been used to generate reliable models of the Fe protein from thermophilic Methanobacter thermoautotrophicus in the analogous structural conformations. The resulting structural comparison reveals that thermal adaptation of the M. thermoautotrophicus Fe protein is conferred by a number of factors, including increased structural rigidity that results from various structural changes within the protein interior. The analysis of hypothetical docking models and nitrogenase complex structures provides insights into the thermal adaptation of the protein-protein interactions that support macromolecular complex formation and catalysis at higher temperatures.

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Section: Resultsmentioning

confidence: 99%

The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus

Sen

Peters

2005

Proteins

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“…In addition to electron transfer, NifH protein performs three more functions. It is involved, along with another seven nif genes, in MoFe cofactor biosynthesis [8,9]. It is also involved in alternative nitrogenase systems regulation.…”

Section: Introductionmentioning

confidence: 99%

Molecular identification of diazotroph microbial consortia in mountain soil

et al. 2010

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Nitrogen fixing microbial consortia from soil samples taken from five altitudinal vegetation zones (alpine, subalpine, coniferous, beech, Maleia flood plain) of Parâng Massif, Romania, were isolated and identified. Molecular characterisation of nitrogen fixing consortia was carried out by PCR and nested PCR with 7 primer sets specific to nifH genes. All nifH genes are specific to nitrogen fixation and are found within phylogenetically related organisms which have the nitrogenase enzyme complex. These molecular studies allowed the assessment of nifH gene diversity within these nitrogen fixing microbial consortia from different type of soils. At high altitude, a consortium of nitrogen fixing bacteria dominated by Azotobacter chroococcum and Azospirillum brasilense was found. Clostridium, Rhizobiales, Herbaspirillum, Frankia species were also found in different rations depending on the altitudinal vegetation zone.

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Compensatory evolution in diploid populations

Ichinose

Iizuka

Kado

et al. 2008

Theoretical Population Biology

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Identification of a second site compensatory mutation in the Fe‐protein that allows diazotrophic growth of Azotobacter vinelandii UW97

Abstract: Azotobacter vinelandii UW97 is defective in nitrogen fixation due to a replacement of serine at position 44 by phenylalanine in the Fe-protein [Pulakat, L., Hausman, B.S.,

Cited by 3 publications

References 46 publications

The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus

The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus

Molecular identification of diazotroph microbial consortia in mountain soil

Compensatory evolution in diploid populations

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