Evidence map›Paper›PMID 11809890›Full record

ArticleNucleic acids research2002

Imino proton NMR analysis of HDV ribozymes: nested double pseudoknot structure and Mg2+ ion-binding site close to the catalytic core in solution.

Yoichiro Tanaka, Tamaki Hori, Mitsuhiro Tagaya, Taiichi Sakamoto, Yasuyuki Kurihara, Masato Katahira, Seiichi Uesugi

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Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

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12citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Yoichiro TanakaDepartment of Environment and Natural Sciences, Graduate School of Environment and Information Sciences, Yokohama National University, 79-7 Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan.
Tamaki Hori
Mitsuhiro Tagaya
Taiichi Sakamoto
Yasuyuki Kurihara
Masato Katahira
Seiichi Uesugi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Minimized trans-acting HDV ribozyme systems consisting of three (Rz-3) and two (Rz-2) RNA strands were prepared and their folding conformations were analyzed by NMR spectroscopy. The guanosine residues in one of the enzyme components of Rz-3 were labeled with 13C and 15N. Imino proton signals were assigned by analysis of NOESY and HSQC spectra. The results are consistent with the nested double pseudoknot model, which contains novel base pairs (P1.1), as observed in the crystal structure of a genomic HDV ribozyme. The NOE connectivities suggest an additional G:G pair at the bottom of P1.1 and at the top of P4. The effects of temperature and Mg2+ ions on base pairs for Rz-3 were examined. The temperature variation experiment on Rz-3 showed that P3 is the most stable and that P1.1 is as stable as P1 and P2. The imino proton signals of the G:U pair at the bottom of P1 and the top of P1.1, which are close to the cleavage site, showed the largest changes upon Mg2+ titration of Rz-3. The results suggest that the catalytic Mg2+ ion binds to the pocket formed by P1 and L3.

Indexed as

Nuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationBase SequenceBinding SitesCatalytic DomainHepatitis Delta VirusMagnesiumModels, MolecularMolecular Sequence DataProtonsRNA, CatalyticSolutionsTemperatureTitrimetryMagnesiumProtonsRNA, CatalyticSolutions

Identifiers

PMID11809890
PMCPMC100292

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.