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AU RNA binding protein/enoyl-CoA hydratase

AUH, 3-methylglutaconyl-CoA hydratase
The methylglutaconyl-CoA hydratase, mitochondrial protein binds to the AU-rich element (ARE), a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. ARE elements are involved in directing RNA to rapid degradation and deadenylation. AUH is also homologous to enol-CoA hydratase, an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is thus a bifunctional chimera between RNA binding and metabolic enzyme activity. A possible subcellular localization in the mitochondria has been demonstrated for the mouse homolog of this protein which shares 92% identity with the human protein. It has been suggested that AUH may have a novel role as a mitochondrial located AU-binding protein. Human AUH is expressed as a single mRNA species of 1.8 kb, and translated as a 40-kDa precursor protein which is subsequently processed to a 32-kDa mature form. [provided by RefSeq, May 2010] (from NCBI)
Top mentioned proteins: ACID, HAD, fibrillin-1, AGE, CAN
Papers on AUH
Metabolic switch during adipogenesis: From branched chain amino acid catabolism to lipid synthesis.
New
Adamski et al., München, Germany. In Arch Biochem Biophys, Feb 2016
Our further analysis led to identification of an enzymatic switch comprising the enzymes Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthase) and Auh (AU RNA binding protein/enoyl-CoA hydratase) which connects leucine degradation with cholesterol synthesis.
Distinct methylation patterns in genes that affect mitochondrial function are associated with kidney disease in blood-derived DNA from individuals with Type 1 diabetes.
New
McKnight et al., Belfast, United Kingdom. In Diabet Med, Aug 2015
Three genes, PMPCB, TSFM and AUH, were observed with differential methylation at multiple Cytosine-phosphate-Guanine sites each (P < 10(-12) ).
Reactivity of Gold Hydrides: O2 Insertion into the Au-H Bond.
New
Bochmann et al., Norwich, United Kingdom. In Organometallics, Jul 2015
UNASSIGNED: Dioxygen reacts with the gold(I) hydride (IPr)AuH under insertion to give the hydroperoxide (IPr)AuOOH, a long-postulated reaction in gold catalysis and the first demonstration of O2 activation by Au-H in a well-defined system.
Enhanced biosynthesis of O-desmethylangolensin from daidzein by a novel oxygen-tolerant cock intestinal bacterium in the presence of atmospheric oxygen.
New
Wang et al., Baoding, China. In J Appl Microbiol, Mar 2015
METHODS AND RESULTS: After a long-term domestication process, an oxygen-tolerant bacterium, which we named Aeroto-AUH-JLC108, was derived from the newly isolated obligate anaerobic bacterium Clostridium sp.
Genotype-based databases for variants causing rare diseases.
Witsch-Baumgartner et al., Innsbruck, Austria. In Gene, 2014
The created databases include ACAD8 (isobutyryl-CoA dehydrogenase deficiency (IBD)), ACADSB (short-chain acyl-CoA dehydrogenase (SCAD) deficiency), AUH (3-methylglutaconic aciduria (3-MGCA)), DHCR7 (Smith-Lemli-Opitz syndrome), HMGCS2 (3-hydroxy-3-methylglutaryl-CoA synthase 2 deficiency), HSD17B10 (17-beta-hydroxysteroid dehydrogenase X deficiency), FKBP14 (Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss; EDSKMH) and ROGDI (Kohlschütter-Tönz syndrome).
Cryotolerance and global gene-expression patterns of Bos taurus indicus and Bos taurus taurus in vitro- and in vivo-produced blastocysts.
Landim-Alvarenga et al., Botucatu, Brazil. In Reprod Fertil Dev, 2014
The lipid metabolism-related genes were upregulated in Simmental (AUH and ELOVL6) and IVP (ACSL3 and ACSL6) blastocysts.
A bifunctional protein regulates mitochondrial protein synthesis.
Filipovska et al., Australia. In Nucleic Acids Res, 2014
The AU-binding homolog of enoyl-coenzyme A (CoA) hydratase (AUH) is a bifunctional protein with RNA-binding activity and a role in leucine catabolism.
Leucine Loading Test is Only Discriminative for 3-Methylglutaconic Aciduria Due to AUH Defect.
Morava et al., Nijmegen, Netherlands. In Jimd Rep, 2013
The "Primary 3-methylglutaconic aciduria," 3-methylglutaconyl-CoA hydratase deficiency or AUH defect, is a disorder of leucine catabolism.
Inborn errors of metabolism with 3-methylglutaconic aciduria as discriminative feature: proper classification and nomenclature.
Review
Wevers et al., Nijmegen, Netherlands. In J Inherit Metab Dis, 2013
One should distinguish between "primary 3-methylglutaconic aciduria" formerly known as type I (3-methylglutaconyl-CoA hydratase deficiency, AUH defect) due to defective leucine catabolism and the--currently known--three groups of "secondary 3-methylglutaconic aciduria".
3-Methylglutaconic aciduria--lessons from 50 genes and 977 patients.
Wevers et al., Nijmegen, Netherlands. In J Inherit Metab Dis, 2013
In 3-methylglutaconyl-CoA hydratase deficiency (mutations in AUH), it derives from leucine degradation.
Involvement of tristetraprolin in transcriptional activation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase by insulin.
Brooks et al., Tampa, United States. In Biochem Biophys Res Commun, 2012
In comparison, siRNA to AU RNA binding protein/enoyl coenzyme A hydratase (AUH) had no effect.
Phenotypic heterogeneity in two siblings with 3-methylglutaconic aciduria type I caused by a novel intragenic deletion.
GeneRIF
Casey et al., Vancouver, Canada. In Mol Genet Metab, 2011
Phenotypic heterogeneity in two siblings with 3-methylglutaconic aciduria type I caused by a novel deletion of exons 1-3 within the AUH gene.
The agmatine-degrading enzyme agmatinase: a key to agmatine signaling in rat and human brain?
GeneRIF
Laube et al., Magdeburg, Germany. In Amino Acids, 2011
Agmatinase activity was predominantly detected in neurons of rat and human brain.
AU-rich RNA-binding induces changes in the quaternary structure of AUH.
GeneRIF
Yokoyama et al., Yokohama, Japan. In Proteins, 2009
The AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU)(24)A.
Cloning and functional expression of a rodent brain cDNA encoding a novel protein with agmatinase activity, but not belonging to the arginase family.
GeneRIF
Carvajal et al., Concepción, Chile. In Arch Biochem Biophys, 2007
Agmatinase activity is adscribed to a novel protein with an active site that promiscuously catalyzes a reaction other than the one it evolved to catalyze.
Biochemical characterization of human 3-methylglutaconyl-CoA hydratase and its role in leucine metabolism.
GeneRIF
Zschocke et al., Mannheim, Germany. In Febs J, 2006
Mutations in the AUH gene are linked to metabolic disease 3-methylglutaconic aciduria type I (MGA1).
Mood stabilizers regulate cytoprotective and mRNA-binding proteins in the brain: long-term effects on cell survival and transcript stability.
Review
K Manji et al., Bethesda, United States. In Int J Neuropsychopharmacol, 2001
In this paper, we describe our recent research endeavours utilizing newer technologies, including a concerted series of mRNA RT-PCR studies, which has led to the identification of novel, hitherto completely unexpected targets for the long-term actions of mood stabilizers - the major cytoprotective protein bcl-2, a human mRNA binding (and stabilizing) protein, AUH, and a Rho kinase.
Screening for defects of branched-chain amino acid metabolism.
Review
Hoffmann et al., Dallas, United States. In Eur J Pediatr, 1993
This report will summarize clinical and metabolite features and enzymological methods available for the diagnosis of the more common defects of branched-chain amino acid metabolism, including isovaleryl-CoA dehydrogenase deficiency, 3-methylcrotonyl-CoA carboxylase deficiency, 3-methylglutaconic aciduria due to 3-methylglutaconyl-CoA hydratase deficiency and other less well characterized defects, 3-hydroxy-3-methylglutaryl-CoA lyase deficiency, and 2-methylacetoacetyl-CoA thiolase deficiency.
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