ArticleRNA (New York, N.Y.)2005
Differences and similarities between Drosophila and mammalian 3' end processing of histone pre-mRNAs.
Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- A region of SLBP outside the mRNA-processing domain is essential for deposition of histone mRNA into theJournal of cell science · 2021Article
- Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery.Methods in enzymology · 2021Article
- Composition and processing activity of a semi-recombinant holo U7 snRNP.Nucleic acids research · 2020Article
- Biallelic sequence variants in INTS1 in patients with developmental delays, cataracts, and craniofacial anomalies.European journal of human genetics : EJHG · 2019Article
- Article
- Protein composition of catalytically active U7-dependent processing complexes assembled on histone pre-mRNA containing biotin and a photo-cleavable linker.Nucleic acids research · 2018Article
- U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein.RNA (New York, N.Y.) · 2017Article
- EnD-Seq and AppEnD: sequencing 3' ends to identify nontemplated tails and degradation intermediates.RNA (New York, N.Y.) · 2015Article
- Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors.RNA (New York, N.Y.) · 2013Article
- A subset of Drosophila integrator proteins is essential for efficient U7 snRNA and spliceosomal snRNA 3'-end formation.Molecular and cellular biology · 2011Article
- Article
- A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs.Molecular cell · 2009Article
- Studies of the 5' exonuclease and endonuclease activities of CPSF-73 in histone pre-mRNA processing.Molecular and cellular biology · 2009Article
- U7 snRNAs: a computational survey.Genomics, proteomics & bioinformatics · 2007Article
- Review
- Histone gene expression and histone mRNA 3' end structure in Caenorhabditis elegans.BMC molecular biology · 2007Article
- U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis.RNA (New York, N.Y.) · 2006Article
- 3' Processing of Animal Replication-Dependent Histone mRNAs.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
We used nuclear extracts from Drosophila Kc cells to characterize 3' end processing of Drosophila histone pre-mRNAs. Drosophila SLBP plays a critical role in recruiting the U 7 snRNP to the pre-mRNA and is essential for processing all five Drosophila histone pre-mRNAs. The Drosophila processing machinery strongly prefers cleavage after a fourth nucleotide following the stem-loop and favors an adenosine over pyrimidines in this position. Increasing the distance between the stem-loop and the HDE does not result in a corresponding shift of the cleavage site, suggesting that in Drosophila processing the U 7 snRNP does not function as a molecular ruler. Instead, SLBP directs the cleavage site close to the stem-loop. The upstream cleavage product generated in Drosophila nuclear extracts contains a 3' OH, and the downstream cleavage product is degraded by a nuclease dependent on the U 7 snRNP, suggesting that the cleavage factor has been conserved between Drosophila and mammalian processing. A 2'O-methyl oligonucleotide complementary to the first 17 nt of the Drosophila U 7 snRNA was not able to deplete the U 7 snRNP from Drosophila nuclear extracts, suggesting that the 5' end of the Drosophila U 7 snRNA is inaccessible. This oligonucleotide selectively inhibited processing of only two Drosophila pre-mRNAs and had no effect on processing of the other three pre-mRNAs. Together, these studies demonstrate that although Drosophila and mammalian histone pre-mRNA processing share common features, there are also significant differences, likely reflecting divergence in the mechanism of 3' end processing between vertebrates and invertebrates.
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