1,721,045 research outputs found
Incorporazione di fenilalanina tritiata nei lampbrush chromosomes e nei nucleoli di Triturus vulgaris meridionalis (Anfibi Urodeli)
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Saggio mediante RT-PCR quantitativa per l'attività catalitica in vivo del ribozima di tritone
No full textSviluppo di una tecnica di saggio basata sulla RT-PCR per l'attività catalitica in vivo del ribozima di tritone
No full textEffetti della actinomicina D tritiata sui lampbrush chromosomes di Triturus (Anfibi Urodeli)
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Ulteriori ricerche autoradiografiche sull'incorporazione di H3 fenilalanina nei lampbrush chromosomes di Triturus (Anfibi Urodeli)
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Spontaneous aberrations in lampbrush chromosome XI from a specimen of Triturus vulgaris meridionalis (Amphibia, Urodela).
No full textRNA binding properties and evolutionary conservation of the Xenopus multifinger protein Xfin
No full textXfin is a Xenopus zinc finger protein which is expressed in the cytoplasm of the oocyte and throughout embryogenesis, as well as in the cytoplasm of some specific and highly differentiated cell types (De Lucchini et al., Mech. Dev. 36, 31-40, 1991). In this paper we present a characterization of some structural features of the protein and of its nucleic acid binding properties. We found that Xfin is a phosphoprotein, is present in the soluble fraction of the cytoplasm, and is actively phosphorylated in cytosolic extracts. Several putative phosphorylation sites are present in the cDNA-derived protein sequence, mostly located at specific positions within the Zn-fingers. In an in vitro assay a fusion protein containing part of the finger region of Xfin exhibits specific binding to a poly (G) RNA homopolymer, while it does not bind DNA. The RNA binding activity of the protein is significantly enhanced by phosphorylation. A putative Xfin homolog, which appears to be evolutionarily conserved with regard to size, cytoplasmic expression and antigenic specificity, is present in representatives of five Vertebrate classes. Taken together, these results may suggest that, by virtue of its RNA binding activity modulated through phosphorylation, Xfin could serve some evolutionarily conserved function in post-transcriptional regulation processes
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