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Nuclear Import and the Evolution of a Multifunctional RNA-binding Protein

阅读量：

32

作者：

Rosenblum，S J.

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摘要：

La (SS-B) is a highly expressed protein that is able to bind 3′-oligouridylate and other common RNA sequence/structural motifs. By virtue of these interactions, La is present in a myriad of nuclear and cytoplasmic ribonucleoprotein complexes in vivo where it may function as an RNA-folding protein or RNA chaperone. We have recently characterized the nuclear import pathway of theS. cerevisiaeLa, Lhp1p. The soluble transport factor, or karyopherin, that mediates the import of Lhp1p is Kap108p/Sxm1p. We have now determined a 113-amino acid domain of Lhp1p that is brought to the nucleus by Kap108p. Unexpectedly, this domain does not coincide with the previously identified nuclear localization signal of human La. Furthermore, when expressed inSaccharomyces cerevisiae, the nuclear localization ofSchizosaccharomyces pombe,Drosophila, and human La proteins are independent of Kap108p. We have been able to reconstitute the nuclear import of human La into permeabilized HeLa cells using the recombinant human factors karyopherin α2, karyopherin β1, Ran, and p10. As such, the yeast and human La proteins are imported using different sequence motifs and dissimilar karyopherins. Our results are consistent with an intermingling of the nuclear import and evolution of La.

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关键词：

nuclear transport karyopherin protein evolution RNA biogenesis RNA-binding proteins

DOI：

10.1083/jcb.143.4.887

被引量：

140

年份：

1998

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来源期刊

Journal of Cell Biology
19981116

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2001
被引量：29

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