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In metazoans, most pre-messenger RNAs contain introns that are removed by splicing. The spliced mRNAs are then exported to the cytoplasm. Recent studies showed that splicing promotes efficient mRNA export, but the mechanism for coupling these two processes is not known. Here we show that Aly, the metazoan homologue of the yeast mRNA export factor Yralp (ref. 2), is recruited to messenger ribonucleoprotein (mRNP) complexes generated by splicing. In contrast, Aly does not associate with mRNPs assembled on identical mRNAs that already have no introns or with heterogenous nuclear RNP (hnRNP) complexes. Aly is recruited during spliceosome assembly, and then becomes tightly associated with the spliced mRNP. Aly shuttles between the nucleus and cytoplasm, and excess recombinant Aly increases both the rate and efficiency of mRNA export in vivo. Consistent with its splicing-dependent recruitment, Aly co-localizes with splicing factors in the nucleus. We conclude that splicing is required for efficient mRNA export as a result of coupling between the splicing and the mRNA export machineries. 相似文献
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Journal of Systems Science and Complexity - This study is a detailed analysis of Speculation Game, a simple agent-based model of financial markets, in which the round-trip trading and the dynamic... 相似文献
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D. P. Muehleisen E. J. Katahira R. S. Gray W. E. Bollenbacher 《Cellular and molecular life sciences : CMLS》1994,50(2):159-163
The prothoracicotropic hormones (PTTHs) are cerebral peptides that control insect postembryonic development by stimulating the prothoracic glands to synthesize ecdysteroids. InManduca sexta, the tobacco hornworm, two classes of PTTH are distinguished by their Mr, small (ca. 7 kDa) and big PTTH (ca. 25–30 kDa). Little is known about the physical nature of the PTTHs and this study takes a first step towards defining characteristics of theManduca big PTTH. The neurohormone has a Stokes radius of 2.59 nm and a sedimentation coefficient of 2.76 S. Based on these data, an Mr of 29,443.7 and anf/f
0 of 1.27 were calculated. Combined, the physical data revealManduca big PTTH is an asymmetrical acidic homodimeric peptide with intra- and intermolecular disulfide bonds. 相似文献
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