Sequence and functional characterization of RNase P RNA from the chl <i>a/b</i> containing cyanobacterium <i>Prochlorothrix hollandica</i>

Fingerhut, Christiane; Schön, Astrid

doi:10.1016/s0014-5793(98)00519-5

Cited by 10 publications

(16 citation statements)

References 41 publications

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“…There are published reports that the RNase P RNA from the cyanobacteria Prochlorothrix hollandica and Prochlorococcus marinus are strongly dependent on the presence of CCA in the substrate for activity (31,32), in contradiction with our results. In those studies, a plant chloroplast substrate was used whereas we have used a completely homologous system.…”

Section: Biochemistry: Pascual and Vioquecontrasting

confidence: 99%

“…tRNA genes in cyanobacteria do not code for the 3Ј terminal CCA, and, therefore, it is possible that cyanobacterial RNase P function has evolved in a context in which the CCA sequence is not present. In some cases, an extra helix has been inserted in this region (14,31). The insertion, deletion, or substitution of structures during the evolution of RNase P RNA is widespread.…”

Section: Biochemistry: Pascual and Vioquementioning

confidence: 99%

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Substrate binding and catalysis by ribonuclease P from cyanobacteria and Escherichia coli are affected differently by the 3′ terminal CCA in tRNA precursors

Pascual¹,

Vioque²

1999

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

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We have studied the effect of the 3 terminal CCA sequence in precursors of tRNAs on catalysis by the RNase P RNA or the holoenzyme from the cyanobacterium Synechocystis sp. PCC 6803 in a completely homologous system. We have found that the absence of the 3 terminal CCA is not detrimental to activity, which is in sharp contrast to what is known in other bacterial systems. We have found that this is also true in other cyanobacteria. This situation correlates with the anomalous structure of the J15͞16 loop in cyanobacteria, which is an important loop in the CCA interaction in Escherichia coli RNase P, and with the fact that cyanobacteria do not code the CCA sequence in the genome but add it posttranscriptionally. Modification of nucleotides 330-332 in the J15͞16 loop of Synechocystis RNase P RNA from GGU to CCA has a modest effect on k cat for CCAcontaining substrates and has no effect on cleavage-site selection. We have developed a direct physical assay of the interaction between RNase P RNA and its substrate, which was immobilized on a filter, and we have determined that Synechocystis RNase P RNA binds with better affinity the substrate lacking CCA than the substrate containing it. Our results indicate a mode of substrate binding in RNase P from cyanobacteria that is different from binding in other eubacteria and in which the 3 terminal CCA is not involved.RNase P is a ubiquitous enzyme responsible for generating the 5Ј end of pre-tRNAs by a single endonucleolytic cleavage (1, 2). In bacteria, the enzyme is composed of an RNA subunit and a protein subunit. The RNA subunit is the catalytic component and, under appropriate conditions in vitro, it can cleave substrates in the absence of the protein (3). In addition to all the pre-tRNAs, several other natural and artificial substrates are recognized by RNase P (4-7). Several studies have examined how a single enzyme, generally from Escherichia coli and Bacillus subtilis, can recognize so many different substrates and cleave all of them at the correct position (reviewed in refs. 2, 8, and 9). One of the main conclusions from these studies is the crucial role played by the 3Ј terminal RCCA sequence of pre-tRNAs, where the underlined nucleotides interact with a GGU sequence in the loop connecting helices P15 and P16 (loop J15͞16) (10-12). In addition, the 3Ј terminal CCA participates in binding of Mg 2ϩ ions used in catalysis (13). This interaction is important in defining the cleavage site and reaction rate. In cyanobacteria, the J15͞16 loop has a structure that deviates from the consensus, and it generally lacks a GGU sequence (Fig. 1) (14, 15). In some instances, there is an extra helix inserted in this loop. We have investigated the role of the 3Ј terminal CCA in cyanobacterial pre-tRNAs on cleavage by cyanobacterial RNase P RNA and the holoenzyme. Kinetic analyses indicate that cyanobacteria RNase P has no preference for CCA-containing substrates, as does the E. coli enzyme, under single-or multiple-turnover conditions. The Synechocystis RNase P RNA contain...

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Section: Biochemistry: Pascual and Vioquecontrasting

confidence: 99%

Section: Biochemistry: Pascual and Vioquementioning

confidence: 99%

Substrate binding and catalysis by ribonuclease P from cyanobacteria and Escherichia coli are affected differently by the 3′ terminal CCA in tRNA precursors

Pascual¹,

Vioque²

1999

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

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“…In contrast, the tRNA genes from chloroplasts and other photosynthetic organelles, as well as from cyanobacteria (their phylogenetic ancestors), usually do not encode the CCA‐terminus [32–35]. In striking accordance, RNase P RNAs from primitive plastids and most cyanobacteria are lacking the otherwise highly conserved binding motif [32,36–40], (Fig. 4).…”

Section: Bacterial Rnase Pmentioning

confidence: 99%

“… Two‐dimensional representation of RNase P RNAs from the cyanobacteria P. marinus (A) and P. hollandica (B), where the putative CCA binding motif is boxed. Note that the base pair closing L19 in (B) is inversed compared to [39], where an erroneous structure had been printed. …”

Section: Bacterial Rnase Pmentioning

confidence: 99%

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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“…Prochlorothrix hollandica PCC 9006 contains a rare type of this RNAse characterized by long domain P15/16, as well as by a GGU motif which binds 3 ′ -CCA of pre-tRNA and is absent from the ribozymes of other cyanobacteria (Fingerhut and Schön, 1998). …”

Section: Substrate Assimilation and Enzymologymentioning

confidence: 99%

Cyanobacteria of the Genus Prochlorothrix†

Pinevich¹,

Величко²,

Ivanikova³

2012

Front. Microbio.

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Green cyanobacteria differ from the blue–green cyanobacteria by the possession of a chlorophyll-containing light-harvesting antenna. Three genera of the green cyanobacteria namely Acaryochloris, Prochlorococcus, and Prochloron are unicellular and inhabit marine environments. Prochlorococcus marinus attracts most attention due to its prominent role in marine primary productivity. The fourth genus Prochlorothrix is represented by the filamentous freshwater strains. Unlike the other green cyanobacteria, Prochlorothrix strains are remarkably rare: to date, living isolates have been limited to two European locations. Taking into account fluctuating blooms, morphological resemblance to Planktothrix and Pseudanabaena, and unsuccessful attempts to obtain enrichments of Prochlorothrix, the most successful strategy to search for this cyanobacterium involves PCR with environmental DNA and Prochlorothrix-specific primers. This approach has revealed a broader distribution of Prochlorothrix. Marker genes have been found in at least two additional locations. Despite of the growing evidence for naturally occurring Prochlorothrix, there are only a few cultured strains with one of them (PCC 9006) being claimed to be axenic. In multixenic cultures, Prochlorothrix is accompanied by heterotrophic bacteria indicating a consortium-type association. The genus Prochlorothrix includes two species: P. hollandica and P. scandica based on distinctions in genomic DNA, cell size, temperature optimum, and fatty acid composition of membrane lipids. In this short review the properties of cyanobacteria of the genus Prochlorothrix are described. In addition, the evolutionary scenario for green cyanobacteria is suggested taking into account their possible role in the origin of simple chloroplast.

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Sequence and functional characterization of RNase P RNA from the chl a/b containing cyanobacterium Prochlorothrix hollandica

Cited by 10 publications

References 41 publications

Substrate binding and catalysis by ribonuclease P from cyanobacteria and Escherichia coli are affected differently by the 3′ terminal CCA in tRNA precursors

Substrate binding and catalysis by ribonuclease P from cyanobacteria and Escherichia coli are affected differently by the 3′ terminal CCA in tRNA precursors

Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme

Cyanobacteria of the Genus Prochlorothrix†

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