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Title
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Crystals of X29, a Xenopus laevis U8 snoRNA-binding protein with nuclear decapping activity.
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Authors
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B.A.Peculis,
J.N.Scarsdale,
H.T.Wright.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
1668-1669.
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PubMed id
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Abstract
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Eukaryotic ribosome biosynthesis requires modification (methylation,
pseudouridylation) and nucleolytic processing of precursor ribosomal RNAs in the
nucleolus. The RNA components of the small nucleolar RNPs (snoRNAs) are
essential for many of these events. One snoRNP, called U8, is necessary for
maturation of 5.8S and 28S rRNA in vertebrates. In Xenopus laevis, U8 snoRNA was
found to bind specifically and with high affinity to a protein called X29. X29
is a Nudix hydrolase, a nucleotide diphosphatase that removes the m(7)G and
m(227)G caps from U8 and other RNAs. X29 requires an RNA as substrate and cap
analogues are not substrates or inhibitors of cleavage. To study the
determinants of X29 activity and its specificity for U8 RNA substrate, X29 was
crystallized in an orthorhombic crystal form that diffracts to 2.1 A resolution.
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