Summary
When nuclei are treated with detergents and the chromatin is degraded and removed by subsequent deoxyribonuclease and high salt treatments, a predominantly proteinaceous nuclear substructure, known as the nuclear matrix, remains. Newly synthesized RNA molecules are found to be tightly associated with this nuclear framework. When steady-state hnRNA in adeno-virus-infected cells is analyzed with the S1 mapping procedure, one finds precursors, processing intermediates and products of mRNA processing to be associated with the nuclear matrix. This binding is probably mediated by proteins. In vivo crosslinking experiments and ribonuclease digestions suggest that the hnRNP group āCā proteins might be involved in this association. Analysis of the RNA fragments complexed with the group āCā proteins show that probably more than one of these polypeptides are associated with each molecule of RNA.
Detailed analysis of the splicing of the tripartite leader sequence indicates that several rapid cleavages in the intron regions take place before exon-exon ligation occurs. The unligated pieces of RNA are bound to the nuclear matrix and it is therefore possible that the nuclear matrix provides the structural framework that keeps the pieces of RNA in the correct spatial orientation for ligation.
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Ā© 1985 Martinus Nijhoff Publishing, Boston
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Van Venrooij, W.J., Verheijen, R., Mariman, E.C. (1985). Adenoviral hnRNA is Associated with the Host Nuclear Matrix During Processing. In: Becker, Y., Hadar, J. (eds) Viral Messenger RNA. Developments in Molecular Virology, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2585-7_8
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DOI: https://doi.org/10.1007/978-1-4613-2585-7_8
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