Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2

@article{Beinert1993AconitaseAT,
  title={Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2},
  author={Helmut Beinert and Mary Claire Kennedy},
  journal={The FASEB Journal},
  year={1993},
  volume={7},
  pages={1442 - 1449}
}
In this brief survey, the path of development of our knowledge of the iron‐sulfur enzyme aconitase [citrate(isocitrate)hydrolyase EC4.2.1.3.] is traced from its discovery in 1937, Particular emphasis is on developments in the past decade, when EPR, Mössbauer and electron nuclear double resonance spectroscopies, X‐ray crystallography, and mutational analysis were applied to the problem. More recently discovered was the significant amino acid sequence identity between mitochondrial aconitase and… Expand
Switching aconitase B between catalytic and regulatory modes involves iron‐dependent dimer formation
TLDR
Gel filtration analysis has now shown that cell‐free extracts contain high‐molecular‐weight species of AcnB, and in vitro and in vivo protein interaction experiments have shown thatAcnB forms homodimers, suggesting a simple iron‐mediated dimerization mechanism for switching the AcNB protein between catalytic and regulatory roles. Expand
The solution structure of apo-iron regulatory protein 1.
TLDR
Small angle X-ray scattering was used to determine the low resolution solution structure of apo-IRP1 and to characterize its biophysical properties, and the open Apo- IRP1 conformation seems optimal for subsequent conversion to either functional end state: RNA-binding, or cytosolic aconitase. Expand
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Iron regulatory proteins in pathobiology.
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Iron-Dependent RNA-Binding Activity of Mycobacterium tuberculosis Aconitase
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Thioredoxin Activation of Iron Regulatory Proteins
TLDR
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TLDR
The 2.4 Å structure of E. coli AcnB reveals a high degree of conservation at the active site despite its domain reorganization, and reveals that the additional domain, characteristic of theAcnB subfamily, is a HEAT-like domain, implying a role in protein–protein recognition. Expand
The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways
TLDR
Mechanisms of Fe–S biogenesis and delivery, and methods that will likely reveal important roles of Fe—S proteins in proteins not yet recognized as Fe-S proteins are discussed. Expand
Iron regulatory proteins 1 and 2
  • B. Henderson
  • Biology, Medicine
  • BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1996
TLDR
It is suggested thatIRP‐1 and IRP‐2 may bind preferenitially to certain mRNAs in vivo, possibly extending their known functions beyond the regulation of intracellular iron homeostasis. Expand
Interaction between iron-regulatory proteins and their RNA target sequences, iron-responsive elements.
TLDR
The interaction between the IRPs and the IRE represents one of the best characterised model systems for posttranscriptional gene control, and given that each IRP can also recognise its own unique set of RNAs, the search for new in vivo mRNA targets is expected to provide yet more surprises and insights into the fate of cytoplasmic mRNAs. Expand
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TLDR
It is concluded that the soluble mitochondrial HiPIP is identical with aconitase, and the relationships of iron to labile sulfide, molecular weight and unpaired spins in the EPR signal, and implications for the role of iron in ac onitase are discussed. Expand
Engineering of protein bound iron‐sulfur clusters
An increasing number of iron-sulfur (Fe-S) proteins are found in which the Fe-S cluster is not involved in net electron transfer, as it is in the majority of Fe-S proteins. Most of the former areExpand
Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein.
TLDR
The amino acid composition, molecular weight, isoelectric point, and the sequences of six random peptides clearly show that these physicochemical and structural characteristics are identical to those of IRE-BP, and that c-aconitase is distinctly different from m-aconitic aconitase. Expand
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TLDR
The basic physicochemical data of the enzyme is reinvestigated to arrive at a more precise figure of the stoichiometry of Fe and S2-based on the proposed model of the iron-sulfur cluster of inactive aconitase. Expand
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TLDR
The molar relaxivity, 1/T1p[Fe], for aconitase-bound iron(III) is about half as effective as free iron (III) in relaxing the protons of water, and the inequality of the longitudinal and transverse relaxation rates indicates that protons are rapidly exchanging between bulk solvent and the coordination sphere of the iron( III). Expand
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TLDR
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Summary A brown, soluble protein which, in its oxidized form, has a highly temperature sensitive EPR signal centered at g=2.01 with a width of 25 gauss at 9.2 GHz, was purified from the supernatantExpand
Mutational analysis of active site residues in pig heart aconitase.
TLDR
Results of mutagenesis support the interpretation of the x-ray model, namely that Asp100 and His101 form an ion pair for elimination of the substrate hydroxyl and Ser642 may function as a general base for proton abstraction from citrate or isocitrate in the dehydration step and protonation of cis-aconitate in the hydration step. Expand
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X-ray crystallographic study of the ferredoxin-like protein (iron-sulfur protein III) from Azotobacter vinelandii has been extended to 2.5-A resolution and shows two distinctly different Fe-S clusters. Expand
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The crystal structures of mitochondrial aconitase with isocitrate and nitroisocitrate bound have been solved and refined to R factors of 0.179 and 0.161, respectively, for all observed data in theExpand
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