About: Hairpin structure within the 3′UTR of DNA polymerase β mRNA acts as a post-transcriptional regulatory element and interacts with Hax-1

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About: Hairpin structure within the 3′UTR of DNA polymerase β mRNA acts as a post-transcriptional regulatory element and interacts with Hax-1 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Hairpin structure within the 3′UTR of DNA polymerase β mRNA acts as a post-transcriptional regulatory element and interacts with Hax-1
Creator	Sobczak, Krzysztof Szwarc, Maria Grzybowska, Ewa Sarnowski, Tomasz Siedlecki, Janusz Konopiń Ski, Ryszard Krzy_ Zosiak, Wl--Odzimierz Wilczyń Ska, Anna Zbieta Sarnowska, El_
Source	PMC
abstract	Aberrant expression of DNA polymerase β, a key enzyme involved in base excision repair, leads to genetic instability and carcinogenesis. Pol β expression has been previously shown to be regulated at the level of transcription, but there is also evidence of post-transcriptional regulation, since rat transcripts undergo alternative polyadenylation, and the resulting 3′UTR contain at least one regulatory element. Data presented here indicate that RNA of the short 3′UTR folds to form a strong secondary structure (hairpin). Its regulatory role was established utilizing a luciferase-based reporter system. Further studies led to the identification of a protein factor, which binds to this element—the anti-apoptotic, cytoskeleton-related protein Hax-1. The results of in vitro binding analysis indicate that the formation of the RNA–protein complex is significantly impaired by disruption of the hairpin motif. We demonstrate that Hax-1 binds to Pol β mRNA exclusively in the form of a dimer. Biochemical analysis revealed the presence of Hax-1 in mitochondria, but also in the nuclear matrix, which, along with its transcript-binding properties, suggests that Hax-1 plays a role in post-transcriptional regulation of expression of Pol β.
has issue date	2007-08-17(xsd:dateTime)
bibo:doi	10.1093/nar/gkm502
bibo:pmid	17704138
has license	cc-by-nc
sha1sum (hex)	e3dd1ad4bb9542f0f8fc13f5faab78ee531ae89b
schema:url	https://doi.org/10.1093/nar/gkm502
resource representing a document's title	Hairpin structure within the 3′UTR of DNA polymerase β mRNA acts as a post-transcriptional regulatory element and interacts with Hax-1
has PubMed Central identifier	PMC2018635
has PubMed identifier	17704138
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:e3dd1ad4bb9542f0f8fc13f5faab78ee531ae89b#body_text
is schema:about of	named entity 'demonstrate' named entity 'mRNA' named entity 'base excision repair' named entity 'UTR' covid:arg/e3dd1ad4bb9542f0f8fc13f5faab78ee531ae89b named entity 'Further' named entity 'Aberrant' named entity 'Pol' named entity 'polymerase' named entity 'complex' named entity 'regulated' named entity 'dimer' named entity 'RNA' named entity 'protein' named entity 'regulatory element' named entity 'protein' named entity 'protein complex' named entity 'nuclear matrix' named entity 'regulatory element' named entity 'UTR' named entity 'RNA' named entity 'base excision repair' named entity 'polyadenylation' named entity 'post-transcriptional regulation' named entity 'Biochemical analysis' named entity 'DNA polymerase' named entity 'UTR' named entity 'RNA' named entity 'rat' named entity '1, 2' named entity 'Western blotting' named entity 'polyadenylation' named entity 'dimers' named entity 'UTR' named entity 'protein' named entity 'sigmoidal curve' named entity 'eukaryotic cells' named entity 'cDNA' named entity 'UTR' named entity 'mRNA' named entity 'EcoRI' named entity 'nucleus' named entity 'posttranscriptional' named entity 'UTR' named entity 'mutator phenotype' named entity 'titrated' named entity 'dimer' named entity 'UTR' named entity 'RNA molecule' named entity 'hydrolysis' named entity 'pro-apoptotic' named entity 'subcellular location' named entity 'histidine' named entity 'similar structures' named entity 'plasmids' named entity 'RNAs' named entity 'Roche' named entity 'SDS-PAGE' named entity 'RNase T1' named entity 'RNA' named entity 'microgram' named entity 'vimentin' named entity 'plasmid' named entity 'T7 RNA polymerase' named entity 'Pol' named entity 'cellulose' named entity 'Promega' named entity 'regulatory element' named entity 'cytoskeletal elements' named entity 'Firefly luciferase' named entity 'selenocysteine' named entity 'Tris-HCl' named entity 'Sugo'

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