Processing of precursor particles containing 17S rRNA in a cell free system

Meyhack, Bernd; Meyhack, Irene; Apirion, David

doi:10.1016/0014-5793(74)80515-6

Cited by 20 publications

(8 citation statements)

References 16 publications

(4 reference statements)

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“…An activity responsible for 17-S RNA cleavage has already been described [19]. This activity, tested by incubation of non-purified 27-S particles in different subcellular fractions, was also found on ribosomes but its detachment required washing with higher concentrations (0.3 -0.6 M) of NH4C1 than that (0.2 M) used in our experiments.…”

Section: Discussionsupporting

confidence: 60%

Processing of the 17‐S Escherichia coli Precursor RNA in the 27‐S Pre‐Ribosomal Particle

Hayes

Vasseur

1976

European Journal of Biochemistry

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An RNase activity probably involved in the maturation of 16‐S pre‐ribosomal RNA in Escherichia coli has been partially purified from crude cell extracts. When 27‐S ribosome precursor particles are incubated with this enzyme preparation in vitro, their 17‐S RNA is converted to a product with the same electrophoretic mobility as mature 16‐S rRNA. Fingerprint analysis of this product shows that it contains the 3′‐OH but not the 5′‐P terminus of mature 16‐S rRNA. Generation of the normal 5′‐P terminus seems to require a factor present in cell extracts since incubation of the 27‐S precursor particle in an extract obtained after centrifugation at 30000 g causes conversion of the 17‐S RNA to a 16‐S species containing both termini of mature 16‐S rRNA. Preliminary experiments suggest that correct maturation of the 5′ end of the 17‐S precursor RNA requires a system in which protein synthesis can take place.

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Section: Discussionsupporting

confidence: 60%

Processing of the 17‐S Escherichia coli Precursor RNA in the 27‐S Pre‐Ribosomal Particle

Hayes

Vasseur

1976

European Journal of Biochemistry

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“…The termini of m16, however, are not paired in the p16 molecule; hence, separate 5'and 3'-specific cleavage activities can be envisioned. E. coli RNase M23 and RNase M5 activities have not been detected in vitro, but RNase M16, an activity(ies) which can convert the p16 RNA found in precursor particles to mature-size m16 rRNA, has been described and partially purified (67,68,104). An RNase M16 or M16-like enzyme was subsequently partially purified by Dahlberg et al (33).…”

Section: Microbiol Revmentioning

confidence: 99%

Processing of procaryotic ribonucleic acid.

Gegenheimer¹,

Apirion²

1981

Microbiological Reviews

107

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“…The processing of rRNA transcripts involves a series of post-transcriptional modifications: RNase III, an enzyme specific for double-stranded RNA (11), cleaves the primary transcript, JOS pre-rRNA, into several fragments that are the precursors of 16S (pl7S), 23S (p23S), and 5S (p5S) rRNAs and other fragments that contain the tRNA sequences (6,7,9,12). Additional enzymes are required for the subsequent processing of the cleavage products of RNase III to the mature rRNAs (13)(14)(15)(16)(17).Because the 17S rRNA is longer than the mature 16S rRNA at both the 5' and 3' ends and is undermethylated (18,19), several modifications must occur during the conversion of 17S to 16S rRNA. Hayes and Vasseur (16) described an RNase activity involved in cleavage of the 3' end of 17S rRNA to the mature 3' end of the 16S rRNA; 27S ribosomal precursor particles containing 17S rRNA are the substrate in this reaction.…”

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confidence: 99%

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Processing of the 5' end of Escherichia coli 16S ribosomal RNA.

Dahĺberg¹,

Dahlberg²,

Lund³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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We have isolated and partially characterized an endonuclease involved in processing the 5' end of 16S rRNA of Escherichia coli. A mutant strain that is deficient in this enzyme accumulates a new precursor of 16S rRNA, named 16.3S rRNA. his rRNA has the 3' end of mature 16S rRNA but is about 60 nucleotides longer at theS' end. hi vitro, the enzyme preparation cleaves an RNA fragment of about 60 nucleotides from the 5' end of 16.3S rRNA in 30S ribosomal subunits, yieldin 'the mature 5' end of 16S rRNA. In the mutant strain the 16.3S rRNA is associated with a full complement of 21 ribosomal proteins in 30S subunits. These particles, which comprise 50% of the total 30S subunits, are present on polyribosomes. The rRNA transcription units in Escherichia coli contain the genes for 16S, 23S, and 5S rRNAs and at least four different tRNAs (1-10). The processing of rRNA transcripts involves a series of post-transcriptional modifications: RNase III, an enzyme specific for double-stranded RNA (11), cleaves the primary transcript, JOS pre-rRNA, into several fragments that are the precursors of 16S (pl7S), 23S (p23S), and 5S (p5S) rRNAs and other fragments that contain the tRNA sequences (6,7,9,12). Additional enzymes are required for the subsequent processing of the cleavage products of RNase III to the mature rRNAs (13)(14)(15)(16)(17).Because the 17S rRNA is longer than the mature 16S rRNA at both the 5' and 3' ends and is undermethylated (18,19), several modifications must occur during the conversion of 17S to 16S rRNA. Hayes and Vasseur (16) described an RNase activity involved in cleavage of the 3' end of 17S rRNA to the mature 3' end of the 16S rRNA; 27S ribosomal precursor particles containing 17S rRNA are the substrate in this reaction.In this report we describe an RNase involved in processing of the 5' end of 16S rRNA. A strain of E. coli that lacks the enzyme accumulates a new precursor rRNA, called 16.3S rRNA. We have used 30S particles containing this precursor rRNA as substrate in the isolation of this RNase, which will be called RNase M16. Analysis of in vitro cleavage products made by preparations of this enzyme indicates that it is responsible for the maturation of the 5' end of 16S rRNA. MATERIALS AND METHODSReagents and methods for cell lysis and gel electrophoresis were as described (20)(21)(22) (26)] of E. coli was isolated after incubation of EA2-G1 cells in 1 M hydroxylamine (pH 6) for 20 min at 300 and selection for growth at 420. For preparation of ribosomes, cultures were harvested during the logarithmic phase of growth by rapid cooling on ice, and 30S ribosomal subunits were prepared by sucrose gradient centrifugation.Ribosomal proteins were labeled by growth of 200 ml of cells for two generations at 370 in minimal salts medium containing 50 MCi of "4C-labeled amino acids (EA2 strain) or 250 jsGi of 3H-labeled amino acids (PE strains). Ribosomes were purified as above and the proteins were extracted by acetic acid and separated by two-dimensional gel electrophoresis for quantitation.The 5' ...

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Processing of precursor particles containing 17S rRNA in a cell free system

Cited by 20 publications

References 16 publications

Processing of the 17‐S Escherichia coli Precursor RNA in the 27‐S Pre‐Ribosomal Particle

Processing of the 17‐S Escherichia coli Precursor RNA in the 27‐S Pre‐Ribosomal Particle

Processing of procaryotic ribonucleic acid.

Processing of the 5' end of Escherichia coli 16S ribosomal RNA.

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