ArticleRNA (New York, N.Y.)2001
An unexpected, conserved element of the U3 snoRNA is required for Mpp10p association.
Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Yeast pre-rRNA is processed at the A' site.microPublication biology · 2025Article
- Synergistic defects in pre-rRNA processing from mutations in the U3-specific protein Rrp9 and U3 snoRNA.Nucleic acids research · 2020Article
- Proteins and RNA sequences required for the transition of the t-Utp complex into the SSU processome.FEMS yeast research · 2019Article
- Implication of the box C/D snoRNP assembly factor Rsa1p in U3 snoRNP assembly.Nucleic acids research · 2017Article
- A second base pair interaction between U3 small nucleolar RNA and the 5'-ETS region is required for early cleavage of the yeast pre-ribosomal RNA.Nucleic acids research · 2011Article
- The initial U3 snoRNA:pre-rRNA base pairing interaction required for pre-18S rRNA folding revealed by in vivo chemical probing.Nucleic acids research · 2011Article
- Cross-linking, ligation, and sequencing of hybrids reveals RNA-RNA interactions in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A novel small-subunit processome assembly intermediate that contains the U3 snoRNP, nucleolin, RRP5, and DBP4.Molecular and cellular biology · 2009Article
- The U3 small nucleolar ribonucleoprotein component Imp4p is a telomeric DNA-binding protein.The Biochemical journal · 2007Article
- Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-rRNA) duplexes, possibly to recruit the small subunit processome to the pre-rRNA.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Role of pre-rRNA base pairing and 80S complex formation in subnucleolar localization of the U3 snoRNP.Molecular and cellular biology · 2004Article
- Multimeric threading-based prediction of protein-protein interactions on a genomic scale: application to the Saccharomyces cerevisiae proteome.Genome research · 2003Article
- The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.Nucleic acids research · 2003Article
- Components of an interdependent unit within the SSU processome regulate and mediate its activity.Molecular and cellular biology · 2002Article
- The small subunit processome in ribosome biogenesis—progress and prospects.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The U3 small nucleolar ribonucleoprotein (snoRNP) is composed of a small nucleolar RNA (snoRNA) and at least 10 proteins. The U3 snoRNA base pairs with the pre-rRNA to carry out the A0, A1, and A2 processing reactions that lead to the release of the 18S rRNA from the nascent pre-rRNA transcript. The yeast U3 snoRNA can be divided into a short 5' domain (nt 1-39) and a larger 3' domain (73 to the 3' end) separated by a stretch of nucleotides called the hinge region (nt 40-72). The sequences required for pre-rRNA base pairing are found in the 5' domain and hinge region whereas the 3' domain is largely covered with proteins. Mpp10p, one of the protein components unique to the U3 snoRNP, plays a role in processing at the A1 and A2 sites. Because of its critical role in U3 snoRNP function, we determined which sequences in the U3 snoRNA are required for Mpp10p association. Unlike fibrillarin and all the previous U3 snoRNP components studied in this manner, sequences in the 3' domain are not sufficient for Mpp10p association. Instead, a conserved sequence element in the U3 snoRNA hinge region is required, placing Mpp10p near the 5' domain that carries out the pre-rRNA base-pairing interactions in the functional center of the U3 snoRNP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.