Evolutionary conservation of the U7 small nuclear ribonucleoprotein in<i>Drosophila melanogaster</i>

Azzouz, Teldja N.; Schümperli, Daniel

doi:10.1261/rna.5143303

Cited by 23 publications

(29 citation statements)

References 40 publications

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“…One interaction, which is dispensable for processing involves ZFP100, whereas the other interaction is absolutely essential for processing and may link CPSF-73 to the U7 snRNP (Azzouz et al, 2005a). CPSF-73 is remarkably conserved among evolutionarily distant organisms, whereas Lsm11 has changed over its entire length during evolution and retains only a weak similarity between vertebrates and invertebrates (Azzouz and Schumperli, 2003). Therefore, the recruitment of CPSF-73 by Lsm11 is most likely indirect and may involve a yet unidentified component of the processing machinery.…”

Section: Recruitment Of the Endonucleasementioning

confidence: 99%

“…Drosophila U7 snRNA with 71 nucleotides is the longest known U7 snRNA, contains the noncanonical Sm site (Dominski et al, 2003b) and associates with Lsm10 and Lsm11 (Azzouz and Schumperli, 2003), demonstrating that the structural uniqueness of the Sm complex of the U7 snRNP is also preserved in invertebrates. Because of its length, the 5' end of the U7 snRNA has a larger capacity to form a number of base pairs with each Drosophila histone pre-mRNA (Dominski et al, 2005b).…”

Section: ' End Processing Of Histone Pre-mrnas In Drosophilamentioning

confidence: 99%

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Formation of the 3′ end of histone mRNA: Getting closer to the end

Domiński

Marzluff

2007

Gene

157

180

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Nearly all eukaryotic mRNAs end with a poly (A) tail that is added to their 3' end by the ubiquitous cleavage/polyadenylation machinery. The only known exception to this rule are metazoan replication dependent histone mRNAs, which end with a highly conserved stem-loop structure. This distinct 3' end is generated by specialized 3'end processing machinery that cleaves histone pre-mRNAs 4-5 nucleotides downstream of the stem-loop and consists of the U7 small nuclear RNP (snRNP) and number of protein factors. Recently, the U7 snRNP has been shown to contain a unique Sm core that differs from that of the spliceosomal snRNPs, and an essential heat labile processing factor has been identified as symplekin. In addition, cross-linking studies have pinpointed CPSF-73 as the endonuclease, which catalyzes the cleavage reaction. Thus, many of the critical components of the 3' end processing machinery are now identified. Strikingly, this machinery is not as unique as initially thought but contains a number of factors involved in cleavage/polyadenylation, suggesting that the two mechanisms have a common evolutionary origin. The greatest challenge that lies ahead is to determine how all these factors interact with each other to form a catalytically competent processing complex capable of cleaving histone pre-mRNAs.

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Section: Recruitment Of the Endonucleasementioning

confidence: 99%

Section: ' End Processing Of Histone Pre-mrnas In Drosophilamentioning

confidence: 99%

Formation of the 3′ end of histone mRNA: Getting closer to the end

Domiński

Marzluff

2007

Gene

157

180

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“…Replication-dependent histone mRNAs in Drosophila contain the conserved stem-loop sequence and are cleaved by a processing machinery similar to humans (Dominski et al 2002b(Dominski et al , 2003Azzouz and Schumperli 2003). To address whether histone mRNAs are exported by TAP in vivo, we used an RNAi based approach in Drosophila S2 cells.…”

Section: Depletion Of Tap/nxf1 In Drosophila S2 Cells Blocks Histone mentioning

confidence: 99%

Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP

Erkmann

Sánchez²,

Treichel

et al. 2004

RNA

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Replication-dependent histone mRNAs are the only metazoan mRNAs that are not polyadenylated, ending instead in a conserved stem-loop sequence. Histone pre-mRNAs lack introns and are processed in the nucleus by a single cleavage step, which produces the mature 3 end of the mRNA. We have systematically examined the requirements for the nuclear export of a mouse histone mRNA using the Xenopus oocyte system. Histone mRNAs were efficiently exported when injected as mature mRNAs, demonstrating that the process of 3 end cleavage is not required for export factor binding. Export also does not depend on the stem-loop binding protein (SLBP) since mutations of the stem-loop that prevent SLBP binding and competition with a stem-loop RNA did not affect export. Only the length of the region upstream of the stem-loop, but not its sequence, was important for efficient export. Histone mRNA export was blocked by competition with constitutive transport element (CTE) RNA, indicating that the mRNA export receptor TAP is involved in histone mRNA export. Consistent with this observation, depletion of TAP from Drosophila cells by RNAi resulted in the restriction of mature histone mRNAs to the nucleus.

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“…This region is essential for processing (Pillai et al 2003) and is thought to bind factors unique to histone pre-mRNA processing (Azzouz et al 2005). There is one region within the first 40 amino acids of Lsm11 that is conserved from Drosophila to mammals (Azzouz and Schümperli 2003), although its function is not known.…”

Section: Introductionmentioning

confidence: 99%

Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila

Burch¹,

Godfrey²,

Gasdaska³

et al. 2011

RNA

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Metazoan replication-dependent histone mRNAs are the only nonpolyadenylated cellular mRNAs. Formation of the histone mRNA 39 end requires the U7 snRNP, which contains Lsm10 and Lsm11, and FLASH, a processing factor that binds Lsm11. Here, we identify sequences in Drosophila FLASH (dFLASH) that bind Drosophila Lsm11 (dLsm11), allow localization of dFLASH to the nucleus and histone locus body (HLB), and participate in histone pre-mRNA processing in vivo. Amino acids 105-154 of dFLASH bind to amino acids 1-78 of dLsm11. A two-amino acid mutation of dLsm11 that prevents dFLASH binding but does not affect localization of U7 snRNP to the HLB cannot rescue the lethality or histone pre-mRNA processing defects resulting from an Lsm11 null mutation. The last 45 amino acids of FLASH are required for efficient localization to the HLB in Drosophila cultured cells. Removing the first 64 amino acids of FLASH has no effect on processing in vivo. Removal of 13 additional amino acids of dFLASH results in a dominant negative protein that binds Lsm11 but inhibits processing of histone premRNA in vivo. Inhibition requires the Lsm11 binding site, suggesting that the mutant dFLASH protein sequesters the U7 snRNP in an inactive complex and that residues between 64 and 77 of dFLASH interact with a factor required for processing. Together, these studies demonstrate that direct interaction between dFLASH and dLsm11 is essential for histone pre-mRNA processing in vivo and for proper development and viability in flies.

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Evolutionary conservation of the U7 small nuclear ribonucleoprotein inDrosophila melanogaster

Cited by 23 publications

References 40 publications

Formation of the 3′ end of histone mRNA: Getting closer to the end

Formation of the 3′ end of histone mRNA: Getting closer to the end

Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP

Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila

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