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PUS1 encodes a pseudouridine synthase that converts uridine to pseudouridine once it has been incorporated into an RNA molecule. Zusätzlich bieten wir Ihnen Pseudouridylate Synthase 1 Antikörper (53) und und viele weitere Produktgruppen zu diesem Protein an.
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Collectively, these results suggest that alterations in muscle metabolism related to mitochondrial content and oxidative capacity may account for the reduced exercise capacity in Pus1(-/-) mice.
Results identify a pseudouridine synthase, mPus1p, as a coactivator for retinoic acid receptor (mRAR)gamma when coexpressed with steroid receptor RNA activator.
Pus1p- and Pus3p-dependent pseudouridylation of SRA controls a coactivator-corepressor switch in SRA with major consequences for NR signaling.
results show that the NTD of ERalpha and AR contains a novel RBM that directly binds SRA, and that STR5 can serve as a novel class of RNA inhibitor of ERalpha and AR signaling by interfering with Pus1p-mediated SRA pseudouridylation
Investigation of the sequence and structural requirements for hPus1p activity on human tRNASer.
We identified one novel homozygous null mutation in a familial case. It predicts a nonsense mutation at glutamine 154 (Q154X) that would lead to a protein lacking the 266 C-terminal amino acids
Missense mutation in pseudouridine synthase 1 causes mitochondrial myopathy and sideroblastic anemia
MLASA is associated with absent or greatly reduced tRNA pseudouridylation at specific sites, implicating this pathway in its molecular pathogenesis.
A new homozygous stop mutation (E220X)predicts a protein missing 208/427 amino acid residues on the C terminus. The nuclear isoform has an N-terminal extension absent in the mature mitochondrial isoform.
Three residues (R116, Y173, R267) that correspond to amino acids known to compose the active site of TruA, a bacterial Psi synthase that is homologous to Pus1p, were mutated in human Pus1p.
This gene encodes a pseudouridine synthase that converts uridine to pseudouridine once it has been incorporated into an RNA molecule. The encoded enzyme may play an essential role in tRNA function and in stabilizing the secondary and tertiary structure of many RNAs. A mutation in this gene has been linked to mitochondrial myopathy and sideroblastic anemia. Alternate splicing results in multiple transcript variants.
pseudouridylate synthase 1
, tRNA pseudouridine synthase A, mitochondrial
, tRNA pseudouridine(38-40) synthase
, tRNA pseudouridylate synthase I
, tRNA-uridine isomerase I
, mitochondrial tRNA pseudouridine synthase A
, tRNA uridine isomerase I
, pseudouridine synthase 1