Mg2+ Induces a Sharp and Reversible Transition in U1 and U2 Small Nuclear Ribonucleoprotein Configurations

Reveillaud, Isabelle; Lelay-Taha, M N; Sri-Widada, J.; Brunel, Claude; Jeanteur, P

doi:10.1128/mcb.4.9.1890-1899.1984

Cited by 19 publications

(2 citation statements)

References 24 publications

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“…or with physiological states in vivo, can be important to the function of proteins and nucleic acids. RNA molecules that demonstrate this phenomenon include the leader sequences of trp operon mRNA in Escherichia coli (Lee & Yanofsky, 1977), tRNAs (Crothers & Cole, 1978), rRNAs (Chambliss et al, 1980; Kao & Crothers, 1980), col El primer RNA 0006-2960/86/0425-1205S01.50/0 © 1986 American Chemical Society ( Tomizawa, 1984;Wong & Polisky, 1985), and, possibly, snRNPs (Reveillaud et al, 1984). We have found evidence for a conformational change that, under certain conditions, controls the action of Ml RNA, the catalytic subunit of ribonuclease P from E. coli.…”

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confidence: 99%

M1 RNA, the RNA subunit of Escherichia coli ribonuclease P, can undergo a pH-sensitive conformational change

Altman¹,

Guerrier-Takada²

1986

Biochemistry

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After purification from extracts of whole cells, M1 RNA, the catalytic subunit of ribonuclease P from Escherichia coli, apparently must undergo a change in conformation before it can function catalytically. The rate of this conformational change is dependent upon the duration of incubation at various temperatures and pH. delta E of the transition at pH 7.5 is approximately 36 kcal/mol. The change in conformation is not sensitive to Mg2+ concentration between 10 and 100 mM. A decrease in A260 of M1 RNA in solution has been observed during the incubation period that potentiates the conformational change at 30 degrees C, but no direct correlation can yet be made to specific structural rearrangements.

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mentioning

confidence: 99%

M1 RNA, the RNA subunit of Escherichia coli ribonuclease P, can undergo a pH-sensitive conformational change

Altman¹,

Guerrier-Takada²

1986

Biochemistry

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“…Multiple functions of the cis-spliceosomal U2 snRNP reside in the 5' half of the U2 RNA, which contains stem-loops I and IIa/b separated by a single-stranded region: the 5' end, which is important in spliceosome (complex B) assembly ( 26) and for interacting with U6 RNA during splicing (12,21,53,54); the branch point interaction region between stem-loops I and Ila; and stem-loop Ila, which is essential for splicing in yeast cells (2). In contrast, the 3' half of U2 RNA containing stem-loops III and IV is, with the exception of the Sm motif, dispensable for splicing function (2,19,22,32,39,47); this is surprising since all known U2 snRNP proteins bind within this region: the common Sm protein complex between stem-loops IIb and III (28,43), and both U2-specific proteins A' and B" to stem-loop IV (4,7,45). Protein-protein interactions between the A' and B" proteins appear to be involved in U2-specific recognition of stem-loop IV (15,46).…”

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confidence: 99%

Domain Structure of U2 and U4/U6 Small Nuclear Ribonucleoprotein Particles from Trypanosoma brucei: Identification of trans-Spliceosomal Specific RNA-Protein Interactions

Günzl

Cross

Bindereif

1992

Molecular and Cellular Biology

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Maturation of mRNAs in trypanosomes involves trans splicing of the 5' end of the spliced leader RNA and the exons of polycistronic pre-mRNAs, requiring small nuclear ribonucleoproteins (snRNPs) as cofactors. We have mapped protein-binding sites in the U2 and U4/U6 snRNPs by a combination of RNase H protection analysis, native gel electrophoresis, and CsCl density gradient centrifugation. In the U2 snRNP, protein binding occurs primarily in the 3'-terminal domain; through U2 snRNP reconstitution and chemical modification-interference assays, we have identified discrete positions within stem-loop IV of Trypanosoma brucei U2 RNA that are essential for protein binding; significantly, some of these positions differ from the consensus sequence derived from cis-spliceosomal U2 RNAs. In the U4/U6 snRNP, the major protein-binding region is contained within the 3'-terminal half of U4 RNA. In sum, while the overall domain structure of the U2 and U4/U6 snRNPs is conserved between cis- and trans-splicing systems, our data suggest that there are also trans-spliceosomal specific determinants of RNA-protein binding.

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The cDNA sequences of the sea urchin U7 small nuclear RNA suggest specific contacts between histone mRNA precursor and U7 RNA during RNA processing.

Strub¹,

Galli²,

Busslinger³

et al. 1984

The EMBO Journal

165

128

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3′ Processing of sea urchin H3 histone pre‐mRNA depends on a small nuclear RNP which contains an RNA of nominally 60 nucleotide length, referred to below as U7 RNA. The U7 RNA can be enriched by precipitation of sea urchin U‐snRNPs with human systematic lupus erythematosus antiserum of the Sm serotype. We have prepared cDNA clones of U7 RNA and determined by hybridization techniques that this RNA is present in sea urchin eggs at 30‐fold lower molar concentration than U1 RNA. The RNA sequences derived from an analysis of eight U7 cDNA clones show neither homologies nor complementarities to any other know U‐RNAs. The 3′ portion of the presumptive RNA sequence can be folded into a stem‐loop structure. The 5′‐terminal sequences would be largely unstructured as free RNA. Their most striking feature is their base complementarity to the 3′ conserved sequences of histone pre‐mRNAs. Six out of nine bases of the conserved CAAGAAAGA sequence of the histone mRNA precursor and 13 out of 16 nucleotides from the conserved palindrome can be base paired with presumptive U7 RNA sequence, suggesting a unique hybrid structure for a processing intermediate formed from histone precursor and U7 RNA.

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Mg²⁺ Induces a Sharp and Reversible Transition in U₁ and U₂ Small Nuclear Ribonucleoprotein Configurations

Cited by 19 publications

References 24 publications

M1 RNA, the RNA subunit of Escherichia coli ribonuclease P, can undergo a pH-sensitive conformational change

M1 RNA, the RNA subunit of Escherichia coli ribonuclease P, can undergo a pH-sensitive conformational change

Domain Structure of U2 and U4/U6 Small Nuclear Ribonucleoprotein Particles from Trypanosoma brucei: Identification of trans-Spliceosomal Specific RNA-Protein Interactions

The cDNA sequences of the sea urchin U7 small nuclear RNA suggest specific contacts between histone mRNA precursor and U7 RNA during RNA processing.

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