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Sloan, Katherine E.
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Preferred name
Sloan, Katherine E.
Official Name
Sloan, Katherine E.
Alternative Name
Sloan, K. E.
Sloan, Katherine
Sloan, K.
Sloan, Katherine Elizabeth
Sloan, Katherine E.
Main Affiliation
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2016Journal Article [["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Tollervey, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:07:02Z"],["dc.date.available","2018-11-07T10:07:02Z"],["dc.date.issued","2016"],["dc.format.extent","9016"],["dc.identifier.doi","10.1093/nar/gkw645"],["dc.identifier.isi","000386945000043"],["dc.identifier.pmid","27418679"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39207"],["dc.notes.status","zu prĂĽfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans (vol 44, pg 5399, 2016)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2014Journal Article [["dc.bibliographiccitation.firstpage","540"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","RNA-A PUBLICATION OF THE RNA SOCIETY"],["dc.bibliographiccitation.lastpage","550"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schneider, Claudia"],["dc.contributor.author","Watkins, Nicholas J."],["dc.date.accessioned","2018-11-07T09:42:10Z"],["dc.date.available","2018-11-07T09:42:10Z"],["dc.date.issued","2014"],["dc.description.abstract","During eukaryotic ribosome biogenesis, three of the mature ribosomal (r)RNAs are released from a single precursor transcript (pre-rRNA) by an ordered series of endonucleolytic cleavages and exonucleolytic processing steps. Production of the 18S rRNA requires the removal of the 5 ' external transcribed spacer (5 ' ETS) by endonucleolytic cleavages at sites A0 and A1/site 1. In metazoans, an additional cleavage in the 5 ' ETS, at site A ', upstream of A0, has also been reported. Here, we have investigated how A ' processing is coordinated with assembly of the early preribosomal complex. We find that only the tUTP (UTP-A) complex is critical for A ' cleavage, while components of the bUTP (UTP-B) and U3 snoRNP are important, but not essential, for efficient processing at this site. All other factors involved in the early stages of 18S rRNA processing that were tested here function downstream from this processing step. Interestingly, we show that the RNA surveillance factors XRN2 and MTR4 are also involved in A ' cleavage in humans. A' cleavage is largely bypassed when XRN2 is depleted, and we also discover that A' cleavage is not always the initial processing event in all cell types. Together, our data suggest that A' cleavage is not a prerequisite for downstream pre-rRNA processing steps and may, in fact, represent a quality control step for initial pre-rRNA transcripts. Furthermore, we show that components of the RNA surveillance machinery, including the exosome and TRAMP complexes, also play key roles in the recycling of excised spacer fragments and degradation of aberrant pre-rRNAs in human cells."],["dc.identifier.doi","10.1261/rna.043471.113"],["dc.identifier.isi","000333191300011"],["dc.identifier.pmid","24550520"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33893"],["dc.notes.status","zu prĂĽfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1469-9001"],["dc.relation.issn","1355-8382"],["dc.title","The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2016Journal Article [["dc.bibliographiccitation.firstpage","5399"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5409"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Tollervey, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:12:41Z"],["dc.date.available","2018-11-07T10:12:41Z"],["dc.date.issued","2016"],["dc.description.abstract","During ribosomal RNA (rRNA) maturation, cleavages at defined sites separate the mature rRNAs from spacer regions, but the identities of several enzymes required for 18S rRNA release remain unknown. PilT N-terminus (PIN) domain proteins are frequently endonucleases and the PIN domain protein Utp24 is essential for early cleavages at three pre-rRNA sites in yeast (A0, A1 and A2) and humans (A0, 1 and 2a). In yeast, A1 is cleaved prior to A2 and both cleavages require base-pairing by the U3 snoRNA to the central pseudoknot elements of the 18S rRNA. We found that yeast Utp24 UV-crosslinked in vivo to U3 and the pseudoknot, placing Utp24 close to cleavage at site A1. Yeast and human Utp24 proteins exhibited in vitro endonuclease activity on an RNA substrate containing yeast site A2. Moreover, an intact PIN domain in human UTP24 was required for accurate cleavages at sites 1 and 2a in vivo, whereas mutation of another potential site 2a endonuclease, RCL1, did not affect 18S production. We propose that Utp24 cleaves sites A1/1 and A2/2a in yeast and human cells."],["dc.identifier.doi","10.1093/nar/gkw213"],["dc.identifier.isi","000379753100044"],["dc.identifier.pmid","27034467"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40287"],["dc.notes.status","zu prĂĽfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS