A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

Domiński, Zbigniew; Erkmann, Judith A.; Yang, Xiaocui; Sánchez, Ricardo Mondragón; Marzluff, William F.

doi:10.1101/gad.932302

Cited by 76 publications

(96 citation statements)

References 68 publications

(82 reference statements)

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“…The stem-loop structure is bound by SLBP (stem-loop-binding protein) (also called HBF [hairpin-binding factor]), which helps recruitment of U7 snRNP. A zinc finger protein (ZFP100) bridges SLPB and Lsm11, a component of the U7-snRNP (Dominski et al 2002;Pillai et al 2003). In addition to these, another factor is required for histone pre-mRNA processing.…”

Section: Histone Mrna Terminationmentioning

confidence: 99%

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

291

326

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Gene transcription in the cell nucleus is a complex and highly regulated process. Transcription in eukaryotes requires three distinct RNA polymerases, each of which employs its own mechanisms for initiation, elongation, and termination. Termination mechanisms vary considerably, ranging from relatively simple to exceptionally complex. In this review, we describe the present state of knowledge on how each of the three RNA polymerases terminates and how mechanisms are conserved, or vary, from yeast to human.

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Section: Histone Mrna Terminationmentioning

confidence: 99%

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

291

326

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“…The 3Ј S1 probes for detection of the Drosophila histone H2a and mouse histone H2a-614 mRNAs have been described (Dominski et al 2002a;Lanzotti et al 2002). Hybridization and digestion of DNA-RNA hybrids was carried out essentially as previously described (Ingledue et al 2000;Dominski et al 2002a) using either one oocyte equivalent of each nuclear and cytoplasmic fraction or 1 µg of total RNA.…”

Section: S1 Nuclease Protection Assaymentioning

confidence: 99%

“…Following either a 6-or 8-h incubation period at 18°C, the oocytes were dissected. One oocyte equivalent of RNA from the nuclear and cytoplasmic fractions was subject to an S1 nuclease protection assay (top panel) as described (Ingledue et al 2000;Dominski et al 2002a) or resolved on a denaturing gel to visualize the radiolabeled U6⌬ss snRNA. The migration of the undigested probe and the probe fragment protected by both the H2a wt and ⌬(199-309) mRNAs is indicated to the left of the gel.…”

Section: Shortening the Histone Mrna Reduces Its Rate Of Exportmentioning

confidence: 99%

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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 effect of HBP on processing appears to be mediated by a 100-kD zinc finger protein, ZFP100, that binds to the HBP/hairpin complex (Dominski et al 2002a) and also interacts with the N terminus of the U7 snRNPspecific protein Lsm11 (Pillai et al 2003;see below).…”

Section: Introductionmentioning

confidence: 99%

Evolutionary conservation of the U7 small nuclear ribonucleoprotein inDrosophila melanogaster

Azzouz

Schümperli²

2003

RNA

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The U7 snRNP involved in histone RNA 3 end processing is related to but biochemically distinct from spliceosomal snRNPs. In vertebrates, the Sm core structure assembling around the noncanonical Sm-binding sequence of U7 snRNA contains only five of the seven standard Sm proteins. The missing Sm D1 and D2 subunits are replaced by U7-specific Sm-like proteins Lsm10 and Lsm11, at least the latter of which is important for histone RNA processing. So far, it was unknown if this special U7 snRNP composition is conserved in invertebrates. Here we describe several putative invertebrate Lsm10 and Lsm11 orthologs that display low but clear sequence similarity to their vertebrate counterparts. Immunoprecipitation studies in Drosophila S2 cells indicate that the Drosophila Lsm10 and Lsm11 orthologs (dLsm10 and dLsm11) associate with each other and with Sm B, but not with Sm D1 and D2. Moreover, dLsm11 associates with the recently characterized Drosophila U7 snRNA and, indirectly, with histone H3 pre-mRNA. Furthermore, dLsm10 and dLsm11 can assemble into U7 snRNPs in mammalian cells. These experiments demonstrate a strong evolutionary conservation of the unique U7 snRNP composition, despite a high degree of primary sequence divergence of its constituents. Therefore, Drosophila appears to be a suitable system for further genetic studies of the cell biology of U7 snRNPs.

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A novel zinc finger protein is associated with U7 snRNP and interacts with the stem–loop binding protein in the histone pre-mRNP to stimulate 3′-end processing

Cited by 76 publications

References 68 publications

Transcription termination by nuclear RNA polymerases

Transcription termination by nuclear RNA polymerases

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

Evolutionary conservation of the U7 small nuclear ribonucleoprotein inDrosophila melanogaster

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