In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.

Coilin is known as the marker protein for Cajal bodies (CBs), subnuclear domains important for the biogenesis of small nuclear ribonucleoproteins (snRNPs) which function in pre-mRNA splicing. CBs associate non-randomly with U1 and U2 gene loci, which produce the small nuclear RNA (snRNA) component o...

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Autores principales: Hanna J Broome, Michael D Hebert
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Publicado: Public Library of Science (PLoS) 2012
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Acceso en línea:https://doaj.org/article/24bd3892fa954e779668aadc02bce967
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spelling oai:doaj.org-article:24bd3892fa954e779668aadc02bce9672021-11-18T07:20:17ZIn vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.1932-620310.1371/journal.pone.0036300https://doaj.org/article/24bd3892fa954e779668aadc02bce9672012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22558428/?tool=EBIhttps://doaj.org/toc/1932-6203Coilin is known as the marker protein for Cajal bodies (CBs), subnuclear domains important for the biogenesis of small nuclear ribonucleoproteins (snRNPs) which function in pre-mRNA splicing. CBs associate non-randomly with U1 and U2 gene loci, which produce the small nuclear RNA (snRNA) component of the respective snRNP. Despite recognition as the CB marker protein, coilin is primarily nucleoplasmic, and the function of this fraction is not fully characterized. Here we show that coilin binds double stranded DNA and has RNase activity in vitro. U1 and U2 snRNAs undergo a processing event of the primary transcript prior to incorporation in the snRNP. We find that coilin displays RNase activity within the CU region of the U2 snRNA primary transcript in vitro, and that coilin knockdown results in accumulation of the 3' pre-processed U1 and U2 snRNA. These findings present new characteristics of coilin in vitro, and suggest additional functions of the protein in vivo.Hanna J BroomeMichael D HebertPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e36300 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Hanna J Broome
Michael D Hebert
In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
description Coilin is known as the marker protein for Cajal bodies (CBs), subnuclear domains important for the biogenesis of small nuclear ribonucleoproteins (snRNPs) which function in pre-mRNA splicing. CBs associate non-randomly with U1 and U2 gene loci, which produce the small nuclear RNA (snRNA) component of the respective snRNP. Despite recognition as the CB marker protein, coilin is primarily nucleoplasmic, and the function of this fraction is not fully characterized. Here we show that coilin binds double stranded DNA and has RNase activity in vitro. U1 and U2 snRNAs undergo a processing event of the primary transcript prior to incorporation in the snRNP. We find that coilin displays RNase activity within the CU region of the U2 snRNA primary transcript in vitro, and that coilin knockdown results in accumulation of the 3' pre-processed U1 and U2 snRNA. These findings present new characteristics of coilin in vitro, and suggest additional functions of the protein in vivo.
format article
author Hanna J Broome
Michael D Hebert
author_facet Hanna J Broome
Michael D Hebert
author_sort Hanna J Broome
title In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
title_short In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
title_full In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
title_fullStr In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
title_full_unstemmed In vitro RNase and nucleic acid binding activities implicate coilin in U snRNA processing.
title_sort in vitro rnase and nucleic acid binding activities implicate coilin in u snrna processing.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/24bd3892fa954e779668aadc02bce967
work_keys_str_mv AT hannajbroome invitrornaseandnucleicacidbindingactivitiesimplicatecoilininusnrnaprocessing
AT michaeldhebert invitrornaseandnucleicacidbindingactivitiesimplicatecoilininusnrnaprocessing
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