AU‐rich RNA‐binding induces changes in the quaternary structure of AUH

  title={AU‐rich RNA‐binding induces changes in the quaternary structure of AUH},
  author={Kazuki Kurimoto and Kanako Kuwasako and Alan M. Sandercock and Satoru Unzai and Carol V. Robinson and Yutaka Muto and Shigeyuki Yokoyama},
  journal={Proteins: Structure},
The human AU RNA binding protein/enoyl‐Coenzyme A hydratase (AUH) is a 3‐hydroxy‐3‐methylglutaconyl‐CoA dehydratase in the leucine degradation pathway. It also possesses an RNA‐binding activity to AUUU repeats, which involves no known conserved RNA‐binding domains and is seemingly unrelated to the enzymatic activity. In this study, we performed mass spectrometric analyses to elucidate the oligomeric states of AUH in the presence and absence of RNA. With a short RNA (AUUU) or without RNA, AUH… 

The Structure of LiuC, a 3‐Hydroxy‐3‐Methylglutaconyl CoA Dehydratase Involved in Isovaleryl‐CoA Biosynthesis in Myxococcus xanthus, Reveals Insights into Specificity and Catalysis

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  • B. SuR. Ryan
  • Biology, Computer Science
    Journal of Inherited Metabolic Disease
  • 2013
A path to 3MGA from mitochondrial acetyl CoA is proposed, initiated when syndrome-associated mutations/DNA deletions result in decreased Krebs cycle flux and provides an explanation for the occurrence of 3M GA in multiple disorders associated with compromised mitochondrial function.

The Pseudomonas aeruginosa Isohexenyl Glutaconyl Coenzyme A Hydratase (AtuE) Is Upregulated in Citronellate-Grown Cells and Belongs to the Crotonase Family

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Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA

The crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets is presented, revealing that each triplet is accommodated in a binding pocket formed by β-strands.

Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d

The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3′ untranslated region (3′ UTR) of target mRNAs and promotes their deadenylation and

AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity.

This gene, designated AUH, encodes an RNA binding protein with intrinsic enzymatic activity, suggesting that hydratase and AU-binding functions are located on distinct domains within a single polypeptide.

A 20-amino-acid autonomous RNA-binding domain contained in an enoyl-CoA hydratase.

The identified 20 amino acids constitute an automonous RNA-binding domain, distinct from the RNA-recognition motifs of the family of ribonucleoproteins or NAD/RNA-binding sites in dehydrogenases found in hitherto reported A+U-binding proteins.

Glyceraldehyde-3-phosphate Dehydrogenase Selectively Binds AU-rich RNA in the NAD+-binding Region (Rossmann Fold) (*)

The direct demonstration of AREspecific binding protein activity localized to the NAD+-binding region of GAPDH supports the general concept that enzymes containing this domain may exhibit specific RNA binding activity and play additional roles in nucleic acid metabolism.

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The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule.

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Functional characterization of a non-AUUUA AU-rich element from the c-jun proto-oncogene mRNA: evidence for a novel class of AU-rich elements.

AU-rich RNA-destabilizing elements (AREs) found in the 3' untranslated regions of many labile mRNAs encoding proto-oncoproteins and cytokines generally contain (i) one or more copies of the AUUUA