Structural and functional characterization of mouse U7 small nuclear RNA active in 3' processing of histone pre-mRNA
about
Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanismsPurified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like proteinU7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesisPhosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phaseStem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNABiochemical demonstration of complex formation of histone pre-mRNA with U7 small nuclear ribonucleoprotein and hairpin binding factorsThe low abundance of U7 snRNA is partly determined by its Sm binding siteThe site of 3' end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP3' end processing of mouse histone pre-mRNA: evidence for additional base-pairing between U7 snRNA and pre-mRNAConserved terminal hairpin sequences of histone mRNA precursors are not involved in duplex formation with the U7 RNA but act as a target site for a distinct processing factorA synthetic histone pre-mRNA-U7 small nuclear RNA chimera undergoing cis cleavage in the cytoplasm of Xenopus oocytesAssembly, nuclear import and function of U7 snRNPs studied by microinjection of synthetic U7 RNA into Xenopus oocytes2'-O-methyl, 2'-O-ethyl oligoribonucleotides and phosphorothioate oligodeoxyribonucleotides as inhibitors of the in vitro U7 snRNP-dependent mRNA processing eventNucleotide sequence of the mouse U7 snRNA geneRibozyme, antisense RNA, and antisense DNA inhibition of U7 small nuclear ribonucleoprotein-mediated histone pre-mRNA processing in vitroAdditional low-abundance human small nuclear ribonucleoproteins: U11, U12, etcCloning and characterization of the Drosophila U7 small nuclear RNANMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.Assembly of U7 small nuclear ribonucleoprotein particle and histone RNA 3' processing in Xenopus egg extractsSequence and expression of a mouse U7 snRNA type II pseudogeneU7 snRNAs: a computational surveyLarge-scale sequencing in human chromosome 12p13: experimental and computational gene structure determinationFormation of the 3' end of histone mRNA: getting closer to the endEach of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3'-end processing reactionThe histone genes cluster in Rhynchosciara americana and its transcription profile in salivary glands during larval developmentAntisense Oligonucleotides Promote Exon Inclusion and Correct the Common c.-32-13T>G GAA Splicing Variant in Pompe DiseaseCompilation of DNA sequences of Escherichia coli (update 1990)Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3' end processing in vivo.The histone 3'-terminal stem-loop-binding protein enhances translation through a functional and physical interaction with eukaryotic initiation factor 4G (eIF4G) and eIF33' end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system.Functional importance of conserved nucleotides at the histone RNA 3' processing siteSpecificities of Caenorhabditis elegans and human hairpin binding proteins for the first nucleotide in the histone mRNA hairpin loopDual role for the RNA-binding domain of Xenopus laevis SLBP1 in histone pre-mRNA processingDetection of UV-induced RNA:protein crosslinks in snRNPs by oligonucleotides complementary to the snRNA.Variable effects of the conserved RNA hairpin element upon 3' end processing of histone pre-mRNA in vitro.Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progressionFUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factorsIsolation and characterization of a Drosophila hydei histone DNA repeat unit.The histone mRNA 3' end is required for localization of histone mRNA to polyribosomes.Expression of replication-dependent histone genes in avian spermatids involves an alternate pathway of mRNA 3'-end formation.
P2860
Q22254164-F105D6C2-A9C7-48B6-8388-DB93BF230B49Q24291730-87CE3E40-86C2-4640-B948-CDFC7B577F5AQ24541402-4E4D90E4-C20A-4101-B8E7-BD6A63D81B8AQ24554332-29916A8C-F90B-4169-AED5-FDFBA0D22667Q24554504-C0A1017A-2BEE-490E-BF79-22892FBE8648Q24555701-60341F64-D26D-43FE-BCB6-2FD15B094FB9Q24564682-C8F4D27E-3935-4330-AF13-F0824D1E90E0Q24595569-774C242A-A62F-4D24-B29F-7785C203EC3DQ24605803-0DB2D334-9350-4AF5-91F5-D26EA487FB20Q24612755-69A063C2-6DEC-4289-BEF8-DCD796ADE684Q24623991-103CDD12-31EC-4564-A219-25D20850ACE6Q24624098-190679D3-F601-49BC-8ACE-02350C0DDA11Q24631601-0CE121A2-E604-47B2-97DB-0F03BB087372Q24632249-D017972E-D521-43BE-B9AB-26EAC74EA10AQ24634140-908081DE-4092-4360-9772-832C3CE5CA0AQ24644695-3A1956A1-36A4-4093-BD86-4AA71C89C7C8Q24681285-90258976-AC2F-434B-893C-47AC6F95265DQ27638116-A6235912-BD44-49F1-B3FA-23CDDA50AB87Q28145207-60EE006C-E93C-44A1-BBD7-069C65F59E2AQ28240037-B6BF752A-F4C4-4664-B815-A8B16E073C22Q28268371-A37F99E8-9CE4-4E08-85E0-9D8ECD01AF6EQ28306333-9EEBBB48-20AD-4D0C-8A81-88C0FBBB71ACQ28751417-5543D729-0418-460D-A1F3-367EFBA3AD42Q28776186-69FA333D-3286-4EA0-BF6B-00A7E036A11DQ28818369-2A78B891-9777-4AE4-9709-3F8891B61BFBQ33635367-0743E50F-8BFF-468F-89C2-1F7C60FCD0E1Q33997693-5E1FAF2A-97F8-4B48-A714-E3E17A9B1A26Q34276458-0FD965CB-1B31-4D44-85FE-CC846D862D76Q34303822-D21E3957-4BAD-4348-B22B-38A8A1CBE802Q34324943-77857E9E-63E9-4F27-9AE7-7F46562665C9Q34361303-C045E914-720E-4A11-96C4-9E0A333F9F1EQ34363138-89CDDB5E-C004-475C-B361-F7133F53A420Q34363174-6BB91DEF-738E-4B26-82CA-92382696D6EEQ34974504-D90E29BE-B6C9-450D-A113-12DC1CBE5DC0Q34978310-3D185EFB-2A75-40E6-A60F-722DA6CBA015Q35076429-9891097A-C772-463F-8FA1-684795FB04FEQ35739332-8065B55D-97F6-4C97-9067-625F59C7A8A1Q35833745-57064392-1023-49E5-B24B-ACA1B46FBF07Q35935191-DAC136AB-6F53-4ED4-822E-495FC1A52191Q36767270-BFA58536-19B6-4C39-8FEE-D1D10F478C8C
P2860
Structural and functional characterization of mouse U7 small nuclear RNA active in 3' processing of histone pre-mRNA
description
1988 nî lūn-bûn
@nan
1988 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Structural and functional char ...... processing of histone pre-mRNA
@ast
Structural and functional char ...... processing of histone pre-mRNA
@en
Structural and functional char ...... processing of histone pre-mRNA
@nl
type
label
Structural and functional char ...... processing of histone pre-mRNA
@ast
Structural and functional char ...... processing of histone pre-mRNA
@en
Structural and functional char ...... processing of histone pre-mRNA
@nl
prefLabel
Structural and functional char ...... processing of histone pre-mRNA
@ast
Structural and functional char ...... processing of histone pre-mRNA
@en
Structural and functional char ...... processing of histone pre-mRNA
@nl
P2860
P3181
P356
P1476
Structural and functional char ...... processing of histone pre-mRNA
@en
P2093
D Schümperli
P2860
P304
P3181
P356
10.1128/MCB.8.4.1518
P407
P577
1988-04-01T00:00:00Z