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

Kurimoto K, Kuwasako K, Sandercock AM, Unzai S, Robinson CV, Muto Y, Yokoyama S
Proteins 75 360-72 (2009)
Cited: 8 times
EuropePMC logo PMID: 18831052

Abstract

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 mainly exists as a trimer in solution. On the other hand, the AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)(24)A. AUH was crystallized with the long RNA. Although the RNA was disordered in the crystalline lattice, the AUH structure was determined as an asymmetric dimer of trimers with a kink in the alignment of the trimer axes, resulting in the formation of two clefts with significantly different sizes.

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  1. The Pseudomonas aeruginosa Isohexenyl Glutaconyl Coenzyme A Hydratase (AtuE) Is Upregulated in Citronellate-Grown Cells and Belongs to the Crotonase Family. Poudel N, Pfannstiel J, Simon O, Walter N, Papageorgiou AC, Jendrossek D. Appl Environ Microbiol 81 6558-6566 (2015)
  2. CARDIO-PRED: an in silico tool for predicting cardiovascular-disorder associated proteins. Jain P, Thukral N, Gahlot LK, Hasija Y. Syst Synth Biol 9 55-66 (2015)


Reviews citing this publication (1)

  1. Metabolic biology of 3-methylglutaconic acid-uria: a new perspective. Su B, Ryan RO. J Inherit Metab Dis 37 359-368 (2014)

Articles citing this publication (5)

  1. A Genome-wide CRISPR Screen in Primary Immune Cells to Dissect Regulatory Networks. Parnas O, Jovanovic M, Eisenhaure TM, Herbst RH, Dixit A, Dixit A, Ye CJ, Przybylski D, Platt RJ, Tirosh I, Sanjana NE, Shalem O, Satija R, Raychowdhury R, Mertins P, Carr SA, Zhang F, Hacohen N, Regev A. Cell 162 675-686 (2015)
  2. p32/gC1qR is indispensable for fetal development and mitochondrial translation: importance of its RNA-binding ability. Yagi M, Uchiumi T, Takazaki S, Okuno B, Nomura M, Yoshida S, Kanki T, Kang D. Nucleic Acids Res 40 9717-9737 (2012)
  3. Fetal alcohol syndrome, chemo-biology and OMICS: ethanol effects on vitamin metabolism during neurodevelopment as measured by systems biology analysis. Feltes BC, de Faria Poloni J, Nunes IJ, Bonatto D. OMICS 18 344-363 (2014)
  4. 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. Bock T, Reichelt J, Müller R, Blankenfeldt W. Chembiochem 17 1658-1664 (2016)
  5. Functional identification of microRNA-centered complexes in C. elegans. Hebbar S, Panzade G, Vashisht AA, Wohlschlegel JA, Veksler-Lublinsky I, Zinovyeva AY. Sci Rep 12 7133 (2022)


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