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… 

Switching aconitase B between catalytic and regulatory modes involves iron‐dependent dimer formation

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.

The solution structure of apo-iron regulatory protein 1.

Adrenodoxin: Structure, stability, and electron transfer properties

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Iron-Dependent RNA-Binding Activity of Mycobacterium tuberculosis Aconitase

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The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways

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Iron regulatory proteins 1 and 2

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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.

Interaction between iron-regulatory proteins and their RNA target sequences, iron-responsive elements.

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.
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