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    A nuclear protein in Schizosaccharomyces pombe with homology to the human tumour suppressor Fhit has decapping activity.

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    Authors
    Salehi, Zivar
    Geffers, Lars
    Vilela, Cristina
    Birkenhäger, Ralf
    Ptushkina, Marina
    Berthelot, Karine
    Ferro, Myriam
    Gaskell, Simon J
    Hagan, Iain M
    Stapley, Ben
    McCarthy, John E G
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    Affiliation
    Department of Biomolecular Sciences, UMIST, PO Box 88, Manchester M60 1QD, UK.
    Issue Date
    2002-10
    
    Metadata
    Show full item record
    Abstract
    A number of eukaryotic proteins are already known to orchestrate key steps of mRNA metabolism and translation via interactions with the 5' m7GpppN cap. We have characterized a new type of histidine triad (HIT) motif protein (Nhm1) that co-purifies with the cap-binding complex eIF4F of Schizosaccharomyces pombe. Nhm1 is an RNA-binding protein that binds to m7GTP-Sepharose, albeit with lower specificity and affinity for methylated GTP than is typical for the cap-binding protein known as eukaryotic initiation factor 4E. Sequence searches have revealed that proteins with strong sequence similarity over all regions of the new protein exist in a wide range of eukaryotes, yet none has been characterized up to now. However, other proteins that share specific motifs with Nhm1 include the human Fhit tumour suppressor protein and the diadenosine 5', 5"'-P1, P4-tetraphosphate asymmetrical hydrolase of S. pombe. Our experimental work also reveals that Nhm1 inhibits translation in a cell-free extract prepared from S. pombe, and that it is therefore a putative translational modulator. On the other hand, purified Nhm1 manifests mRNA decapping activity, yet is physically distinct from the Saccharomyces cerevisiae decapping enzyme Dcp1. Moreover, fluorescence and immunofluorescence microscopy show that Nhm1 is predominantly, although not exclusively, nuclear. We conclude that Nhm1 has evolved as a special branch of the HIT motif superfamily that has the potential to influence both the metabolism and the translation of mRNA, and that its presence in S. pombe suggests the utilization of a novel decapping pathway.
    Citation
    A nuclear protein in Schizosaccharomyces pombe with homology to the human tumour suppressor Fhit has decapping activity. 2002, 46 (1):49-62 Mol. Microbiol.
    Journal
    Molecular Microbiology
    URI
    http://hdl.handle.net/10541/84341
    DOI
    10.1046/j.1365-2958.2002.03151.x
    PubMed ID
    12366830
    Type
    Article
    Language
    en
    ISSN
    0950-382X
    ae974a485f413a2113503eed53cd6c53
    10.1046/j.1365-2958.2002.03151.x
    Scopus Count
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    All Paterson Institute for Cancer Research

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