Literature DB >> 28853924

Regulation by 3'-Untranslated Regions.

Christine Mayr1.   

Abstract

3'-untranslated regions (3'-UTRs) are the noncoding parts of mRNAs. Compared to yeast, in humans, median 3'-UTR length has expanded approximately tenfold alongside an increased generation of alternative 3'-UTR isoforms. In contrast, the number of coding genes, as well as coding region length, has remained similar. This suggests an important role for 3'-UTRs in the biology of higher organisms. 3'-UTRs are best known to regulate diverse fates of mRNAs, including degradation, translation, and localization, but they can also function like long noncoding or small RNAs, as has been shown for whole 3'-UTRs as well as for cleaved fragments. Furthermore, 3'-UTRs determine the fate of proteins through the regulation of protein-protein interactions. They facilitate cotranslational protein complex formation, which establishes a role for 3'-UTRs as evolved eukaryotic operons. Whereas bacterial operons promote the interaction of two subunits, 3'-UTRs enable the formation of protein complexes with diverse compositions. All of these 3'-UTR functions are accomplished by effector proteins that are recruited by RNA-binding proteins that bind to 3'-UTR cis-elements. In summary, 3'-UTRs seem to be major players in gene regulation that enable local functions, compartmentalization, and cooperativity, which makes them important tools for the regulation of phenotypic diversity of higher organisms.

Entities:  

Keywords:  RNA-binding proteins; accessibility of regulatory elements; alternative 3′-UTRs; alternative polyadenylation; cellular organization; cooperativity; cotranslational protein complex formation; mRNA localization; noncoding RNA; regulatory RNA

Mesh:

Substances:

Year:  2017        PMID: 28853924     DOI: 10.1146/annurev-genet-120116-024704

Source DB:  PubMed          Journal:  Annu Rev Genet        ISSN: 0066-4197            Impact factor:   16.830


  151 in total

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8.  Regulation of the Ysh1 endonuclease of the mRNA cleavage/polyadenylation complex by ubiquitin-mediated degradation.

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