Localization and expression of the closely linked cyanelle genes for RNase P RNA and two transfer RNAs

Baum, Michaël; Schön, Astrid

doi:10.1016/0014-5793(96)00148-2

Cited by 13 publications

(7 citation statements)

References 32 publications

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“…[22, 23]). In contrast to E. coli , tRNA genes from cyanobacteria and plastids do not encode the terminal CCA sequence [6, 18, 24, 25]. In accordance, a motif corresponding to the well‐conserved CCA‐binding site in most other RNase P RNAs [26–29]is only found in a small subset of the known cyanobacterial sequences [13–17].…”

Section: Introductionmentioning

confidence: 89%

RNase P RNA from Prochlorococcus marinus: contribution of substrate domains to recognition by a cyanobacterial ribozyme

1998

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The molecular organisation of the Prochlorococcus marinus rnpB gene and the catalytic activity of the encoded RNA were characterised. Kinetic parameters for several pre-tRNA substrates were comparable to those from other eubacterial RNase P RNAs, although unusually high cation concentrations were required. The CCA-end of pre-tRNAs is essential for efficient turnover despite the lack of the canonical binding motif in P. marinus RNase P RNA. A trnR gene is located only 38 nt upstream the rnpB 5P end on the complementary strand. This arrangement resembles those in the plastids of Cyanophora and Porphyra but not in any other bacterium.z 1998 Federation of European Biochemical Societies.

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Section: Introductionmentioning

confidence: 89%

RNase P RNA from Prochlorococcus marinus: contribution of substrate domains to recognition by a cyanobacterial ribozyme

1998

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“…The plasmid obtained, after digestion with Dra I, was used for in vitro run‐off transcription with T7 RNA polymerase [9]. The RNAs obtained would contain the same ends and sequence as those expected for the authentic cyanelle P RNA [10]except for the extra G at the 5′ end.…”

Section: Methodsmentioning

confidence: 99%

Functional reconstitution of RNase P activity from a plastid RNA subunit and a cyanobacterial protein subunit

Pascual

Vioque

1999

FEBS Letters

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The plastid (cyanelle) from the Glaucocystophyceae alga Cyanophora paradoxa contains an RNase P RNA subunit (P RNA) similar to the cyanobacterial P RNA. We have synthesized this RNA by in vitro transcription and analyzed its activity in the absence or presence of the RNase P protein subunit (P protein) from Escherichia coli and the cyanobacterium Synechocystis sp. PCC 6803. In contrast to the bacterial P RNA, the cyanelle P RNA is not active in the absence of protein in any of the conditions tested. A functional enzyme could be reconstituted with the Synechocystis protein but not with the E. coli protein. This is the first demonstration of RNase P activity reconstitution from organellar and bacterial subunits.z 1999 Federation of European Biochemical Societies.

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“…The photosynthetic organelle (cyanelle) of C. paradoxa occupies a bridge position in the plastid evolution, combining properties of free‐living cyanobacteria and modern chloroplasts. The cyanelle genome encodes a RNase P RNA which conforms to the A‐type bacterial structure and is an integral and essential component of the organellar RNase P ([36,128], see Fig. 1A).…”

Section: Rnase P From Photosynthetic Organellesmentioning

confidence: 99%

“…5. In the cyanelle, two tRNA genes are directly flanking rnpB on the opposite DNA strand [128]. In the red alga, several protein genes are interspersed between the RNA genes.…”

Section: Rnase P From Photosynthetic Organellesmentioning

confidence: 99%

“… Organisation of the genomic region surrounding rnpB. The circular plastomes of P. purpurea (Por), C. paradoxa (Cya) and the liverwort Marchantia polymorpha (Mpo) are represented in linear form, opened within the small single copy region [34,128]. Only a small portion of the genome is shown for the cyanobacterium P. marinus [40].…”

Section: Rnase P From Photosynthetic Organellesmentioning

confidence: 99%

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Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme

Schön

1999

FEMS Microbiol Rev

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Ribonuclease P is the endonuclease required for generating the mature tRNA 5'-end. The ribonucleoprotein character of this enzyme has now been proven in most organisms and organelles. Exceptions, however, are still the chloroplasts, plant nuclei and animal mitochondria where no associated RNAs have been detected to date. In contrast to the known RNA subunits, which are fairly well-conserved in size and structure among diverse phylogenetic groups, the protein contribution to the holoenzyme is highly variable in size and number of the individual components. The structure of the bacterial protein component has recently been solved. In contrast, the spatial arrangement of the multiple subunits in eukaryotic enzymes is still enigmatic. Substrate requirements of the enzymes or their catalytic RNA subunits are equally diverse, ranging from simple single domain mimics to an almost intact three-dimensional structure of the pre-tRNA substrate. As an example for an intermediate in the enzyme evolution, ribonuclease P from the Cyanophora paradoxa cyanelle will be discussed in more detail. This enzyme is unique, as it combines cyanobacterial and eukaryotic features in its function, subunit composition and holoenzyme topology.

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Localization and expression of the closely linked cyanelle genes for RNase P RNA and two transfer RNAs

Cited by 13 publications

References 32 publications

RNase P RNA from Prochlorococcus marinus: contribution of substrate domains to recognition by a cyanobacterial ribozyme

RNase P RNA from Prochlorococcus marinus: contribution of substrate domains to recognition by a cyanobacterial ribozyme

Functional reconstitution of RNase P activity from a plastid RNA subunit and a cyanobacterial protein subunit

Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme

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