| http://purl.uniprot.org/citations/28490506 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28490506 | http://www.w3.org/2000/01/rdf-schema#comment | "The role of many enzymes extends beyond their dedicated catalytic activity by fulfilling important cellular functions in a catalysis-independent fashion. In this aspect, little is known about 3'-end RNA-modifying enzymes that belong to the class of nucleotidyl transferases. Among these are noncanonical poly(A) polymerases, a group of evolutionarily conserved enzymes that are critical for gene expression regulation, by adding adenosines to the 3'-end of RNA targets. In this study, we investigate whether the functions of the cytoplasmic poly(A) polymerase (cytoPAP) GLD-2 in C. elegans germ cells exclusively depend on its catalytic activity. To this end, we analyzed a specific missense mutation affecting a conserved amino acid in the catalytic region of GLD-2 cytoPAP. Although this mutated protein is expressed to wild-type levels and incorporated into cytoPAP complexes, we found that it cannot elongate mRNA poly(A) tails efficiently or promote GLD-2 target mRNA abundance. Furthermore, germ cell defects in animals expressing this mutant protein strongly resemble those lacking the GLD-2 protein altogether, arguing that only the polyadenylation activity of GLD-2 is essential for gametogenesis. In summary, we propose that all known molecular and biological functions of GLD-2 depend on its enzymatic activity, demonstrating that polyadenylation is the key mechanism of GLD-2 functionality. Our findings highlight the enzymatic importance of noncanonical poly(A) polymerases and emphasize the pivotal role of poly(A) tail-centered cytoplasmic mRNA regulation in germ cell biology."xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.org/dc/terms/identifier | "doi:10.1261/rna.061473.117"xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/author | "Eckmann C.R."xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/author | "Nousch M."xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/author | "Minasaki R."xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/name | "RNA"xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/pages | "1180-1187"xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/title | "Polyadenylation is the key aspect of GLD-2 function in C. elegans."xsd:string |
| http://purl.uniprot.org/citations/28490506 | http://purl.uniprot.org/core/volume | "23"xsd:string |
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