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HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5 '-phosphatase

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Preumont, Alice [UCL] Rzem, Rim [UCL] Vertommen, Didier [UCL] Van Schaftingen, Emile [UCL]

Pseudouridine. the fifth-most abundant nucleoside in RNA, is not metabolized in mammals. but is excreted intact in urine The purpose of the present work was to search for an enzyme that would dephosphorylate pseudouridine 5'-phosphate, a potential intermediate in RNA degradation We show that human erythrocytes contain a pseudouridine-5'-phosphatase displaying a K-m <= mu M for its substrate The activity of the partially purified enzyme was dependent on Mg2+, and was inhibited by Ca2+ and vanadate. suggesting that it belonged to the 'haloacid dehalogenase' family of phosphatases. Its low molecular mass (26 kDa) suggested that this phosphatase could correspond to the protein encoded by the HDHD1 (haloacid dehalogenase-like hydrolase domain-containing 1) gene, present next to the STS (steroid sulfatase) gene on human chromosome Xp22. Purified human recombinant I-I D I dephosphorylated pseudouridine 5'-phosphate with a k(cat) of 1 6 s(-1). a K-m 0.3 mu M and a catalytic efficiency at least 1000-fold higher than that or which it acted on other phosphate esters, including 5'-UMP. The molecular identity of pseudouridine-5'-phosphatase was confirmed by the finding that its activity was negligible (<10% of controls) in extracts of B-cell lymphoblasts or erythrocytes both X-linked ichthyosis patients harbouring a combined deletion of the STS gene (the X-linked ichthyosis gene) and the HDHD1 Furthermore, pseudouridine-5'-phosphatase activity was 1.5-fold higher in erythrocytes from women compared with men, in agreement with the HDHD1 gene undergoing only partial inactivation in females In conclusion, HDHD1 is a phosphatase specifically involved in dephosphorylation of a modified nucleotide present in RNA

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès restreint
Publication date 2010
Language Anglais
Journal information "Biochemical Journal" - Vol. 431, no. 2, p. 237-244 (2010)
Peer reviewed yes
Publisher Portland Press Ltd. ((United Kingdom) London)
issn 0264-6021
e-issn 1470-8728
Publication status Publié
Affiliations UCL - SSS/DDUV - Institut de Duve
UCL - SSS/DDUV/PHOS - Protein phosphorylation
MESH Subject Substrate Specificity ; Sex Characteristics ; Sequence Homology, Amino Acid ; Sequence Alignment ; Recombinant Proteins - metabolism ; Pseudouridine ; Proteins - chemistry - genetics - metabolism ; Phosphoric Monoester Hydrolases - chemistry - isolation & purification - metabolism ; Molecular Sequence Data ; Male ; Ichthyosis, X-Linked - enzymology - genetics ; Humans ; Gene Deletion ; Female ; Esters - metabolism ; Erythrocytes - enzymology ; Chromatography, Ion Exchange ; Chromatography, Gel ; Cell Line ; Cell Extracts ; Amino Acid Sequence ; Adenosine - metabolism
Keywords haloacid dehalogenase-like hydrolase domain-containing 1 (HDHD1) ; ichthyosis ; nucleotidase ; phosphatase ; pseudouridine ; RNA metabolism
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Bibliographic reference Preumont, Alice ; Rzem, Rim ; Vertommen, Didier ; Van Schaftingen, Emile. HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5 '-phosphatase. In: Biochemical Journal, Vol. 431, no. 2, p. 237-244 (2010)
Permanent URL http://hdl.handle.net/2078.1/34994