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Titolo:
Monitoring the structure of Escherichia coli RNase P RNA in the presence of various divalent metal ions
Autore:
Brannvall, M; Mikkelsen, NE; Kirsebom, LA;
Indirizzi:
Biomed Ctr, Dept Cell & Mol Biol, SE-75124 Uppsala, Sweden Biomed Ctr Uppsala Sweden SE-75124 & Mol Biol, SE-75124 Uppsala, Sweden
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 7, volume: 29, anno: 2001,
pagine: 1426 - 1432
SICI:
0305-1048(20010401)29:7<1426:MTSOEC>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEAD-CATALYZED CLEAVAGE; YEAST TRANSFER RNAPHE; GROUP-I INTRON; RIBONUCLEASE-P; M1 RNA; MAGNESIUM-IONS; TETRAHYMENA RIBOZYME; TERTIARY INTERACTION; SITE SELECTION; ACTIVE-SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Kirsebom, LA Biomed Ctr, Dept Cell & Mol Biol, Box 596, SE-75124 Uppsala, Sweden Biomed Ctr Box 596 Uppsala Sweden SE-75124 4 Uppsala, Sweden
Citazione:
M. Brannvall et al., "Monitoring the structure of Escherichia coli RNase P RNA in the presence of various divalent metal ions", NUCL ACID R, 29(7), 2001, pp. 1426-1432

Abstract

Lead(II)-induced cleavage can be used as a tool to probe conformational changes in RNA, In this report, we have investigated the conformation of M1 RNA, the catalytic subunit of Escherichia coli RNase P, by studying the lead(II)-induced cleavage pattern in the presence of various divalent metal ions. Our data suggest that the overall conformation of M1 RNA is very similarin the presence of Mg2+, Mn2+, Ca2+, Sr2+ and Ba2+, while it is changed compared to the Mg2+-induced conformation in the presence of other divalent metal ions, Cd2+ for example, We also observed that correct folding of some M1 RNA domains is promoted by Pb2+, while folding of other domain(s) requires the additional presence of other divalent metal ions, cobalt(III) hexamine or spermidine. Based on the suppression of Pb2+ cleavage at increasing concentrations of various divalent metal ions, our findings suggest that different divalent metal ions bind with different affinities to M1 RNA as wellas to an RNase P hairpin-loop substrate and yeast tRNA(Phe). We suggest that this approach can be used to obtain information about the relative binding strength for different divalent metal ions to RNA in general, as well asto specific RNA divalent metal ion binding sites. Of these studied in thisreport, Mn2+ is generally among the strongest RNA binders.

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Documento generato il 04/04/20 alle ore 02:55:02