2013
DOI: 10.1261/rna.040360.113
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3′-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors

Abstract: 3′ -End cleavage of animal replication-dependent histone pre-mRNAs is controlled by the U7 snRNP. Lsm11, the largest component of the U7-specific Sm ring, interacts with FLASH, and in mammalian nuclear extracts these two proteins form a platform that recruits the CPSF73 endonuclease and other polyadenylation factors to the U7 snRNP. FLASH is limiting, and the majority of the U7 snRNP in mammalian extracts exists as a core particle consisting of the U7 snRNA and the Sm ring. Here, we purified the U7 snRNP from … Show more

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Cited by 49 publications
(93 citation statements)
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References 69 publications
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“…In Drosophila, there is no histone pre-mRNA cleavage until dSLBP binds (10). The free phosphorylated C-terminal tail of dSLBP could assist in assembling a processing complex after it has promoted binding to the stemloop RNA.…”
Section: Discussionmentioning
confidence: 99%
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“…In Drosophila, there is no histone pre-mRNA cleavage until dSLBP binds (10). The free phosphorylated C-terminal tail of dSLBP could assist in assembling a processing complex after it has promoted binding to the stemloop RNA.…”
Section: Discussionmentioning
confidence: 99%
“…In mammalian nuclear extracts, SLBP is not absolutely required for the biochemical reaction of processing (12). In contrast, cleavage of histone pre-mRNA in Drosophila cells and nuclear extracts requires the binding of SLBP to the stem loop (10,13).…”
mentioning
confidence: 97%
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“…Taking advantage of our knowledge of the molecular interactions of HLB components, 44,70,72,73,[99][100][101] we have performed genetic studies in Drosophila using mutant proteins that are either processing defective or unable to localize to the HLB. Unlike other metazoan genes, where transcription can continue well 3 0 of the polyadenylation site, transcription termination is tightly coupled to histone mRNA processing in both Drosophila and mammals.…”
Section: Hlb Functionmentioning
confidence: 99%
“…FLASH and Lsm11 interact to form a protein surface that recruits a set of proteins termed the histone cleavage complex (HCC). 100,101 The HCC includes the endonuclease core of the CPSF polyadenylation complex (CPSF73 and CPSF100) plus the protein Symplekin, which binds CstF64. The Symplekin/CstF64 interaction is likely specific for histone pre-mRNA processing, since CstF64 forms a complex with CstF77 and CstF50 that functions in polyadenylation using the same region it uses to interact with Symplekin.…”
Section: Knockdown Of Y3mentioning
confidence: 99%