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Cited by 175

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli

Guerrier-Takada, Cecilia, Haydock, Karen, Allen, Leland, Altman, Sidney·1986·Biochemistry

Abstract

M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli, can under certain conditions catalytically cleave precursors to tRNA in the absence of C5, the protein moiety of RNase P. M1 RNA itself is not cleaved during the reaction, nor does it form any covalent bonds with its substrate. Only magnesium and, to a lesser extent, manganese ions can function at the catalytic center of M1 RNA. Several other ions either inhibit the binding of magnesium ion at the active site or function as structural counterions. The reaction rate of cleavage of precursors to tRNAs by M1 RNA is enhanced in the presence of poly-(ethylene glycol) or 2-methyl-2,4-pentanediol. Many aspects of the reaction catalyzed by M1 RNA are compatible with a mechanism in which phosphodiester bond cleavage is mediated by metal ion.

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Crossref · 10.1021/bi00355a006

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Metadata

Authors
Guerrier-Takada, C., Haydock, K., Allen, L., & Altman, S.
Venue
Biochemistry
Published
1986-04-08
Volume
25
Issue
7
Pages
1509-1515
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
OpenAlex
W1978847377
Cited by
175
References
1
FWCI
4.56
Type
journal article
Language
en
Open access
closed

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