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Organizacja i funkcja ciałek Cajala

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Summary There ismuch interest in recent years in the possible role of different nuclear bodies (NBs) in cellular functions. NBs include the well-characterized Cajal bodies (CBs; or coiled bodies), which were first described in vertebrate neurons by Ramón y Cajal nearly 100 years ago and since then demonstrated in a variety of organisms and cell types, including both animals and plants. Cajal bodies contain C snurposomes with their associated B snurposomes. Many discussions of CB function emphasize their possible involvement in assembly, modification, or storage of RNA processing factors, especially small nucleolar ribonucleoprotein particles (snoRNPs), splicing small nuclear ribonucleoprotein particles (snRNPs), and the U7 snRNP. Moreover, some evidence suggests that CBs play an even wider role in transcription. Taking into account the composition of CBs and the targeting of various transcription and processing factors to CBs, we conclude that theymay be the primary site for assembly of the transcription machinery of the nucleus. The objective of this article is to summarize some aspects of these nuclear bodies, including their proposed roles in cells and in human diseases.
EN
Summary Adenosine deaminases that act on RNA (ADARs) convert adenosine to inosine in double-stranded regions of RNA via hydrolytic deamination. As inosines are recognized as guanosines during translation this editing event can lead to a codon exchange in the edited mRNA. The amino acid changes introduced by this A-to-I RNA editing result in significant alterations in the physiological properties of gene products. For instance, editing of the "Q/R" site of AMPA GluR-B subunit dramatically decreases the Ca+2 permeability of the channel. Dramatic changes in the G-protein coupling efficiency of 5-HT2CR as well as in the rates of KV2K1 channel closure have been reported to be consequences of A-to-I RNA editing also. In addition, creation of an alternative splice acceptor site via editing of its own mRNA by ADAR2 has been reported. The A-to-I RNA editing mechanism requires: (1) a doublestranded RNA (dsRNA) structure, usually formed between the exonic editing site and a downstream intron sequence and (2) dsRNA-specific adenosine deaminases. The members of this ADAR gene family appear to share structural similarity, containing two to three repeats of dsRNA-binding domains and a separate deaminase or catalytic domain. Defects in ADAR are a cause of some diseases, for example dyschromatosis symmetrica hereditaria.
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