Partial purification and characterization of RNase P from human peripheral lymphocytes

Vourekas, Anastassios; Vryzaki, Eleftheria; Toumpeki, Chrisavgi; Stamatopoulou, Vassiliki; Monastirli, Alexandra; Tsambaos, D.; Drainas, Denis

doi:10.1111/j.1600-0625.2008.00772.x

Cited by 4 publications

(3 citation statements)

References 17 publications

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“…23 Furthermore, the kinetic constants K m (120 nM) and k cat (4.7 min −1 ) appear to be in the same range of those reported for RNase P enzymes from other bacteria and eukarya. 24,25 Biochemical characterization of Zmo wtRPR and Zmo ΔP19RPR in the absence of a protein cofactor revealed temperature and pH optima identical to those of the holoezyme, but monovalent and divalent cation requirements for optimal activity are considerably elevated (Figure 2). P19 seems to be an integral part of the overall fold of the Zmo RPR, contributing significantly to the stabilization of the active conformation.…”

Section: ■ Discussionmentioning

confidence: 99%

On the Role of the Appended P19 Element in Type A RNAs of Bacterial RNase P

et al. 2014

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Comparative in silico analyses of bacterial RNase P enzymes clustered their RNA subunits in type A RNA, found in Escherichia coli, and in type B, found in Bacillus subtilis. Zymomonas mobilis RNase P consists of one protein (Zmo-RnpA) and one type A RNA (RPR) subunit containing the P19 element, present in many RNase P RNAs of any structure class but lacking in the E. coli RNase P RNA. To investigate the putative role of the P19 stem, we constructed a P19 deletion RNA mutant (ΔP19RPR) and performed detailed kinetic analysis of reconstituted enzymes in the presence of the homologous Zmo-RnpA protein or Eco-RnpA protein from E. coli. The deletion of P19 perturbs the monovalent ion requirements. The Mg(2+) requirement for the ΔP19RPR holoenzyme was almost identical to that for the wtRPR holoenzyme at Mg(2+) concentrations of ≤25 mM. Interestingly, enzymes reconstituted with Eco-RnpA protein, relative to those assembled with Zmo-RnpA, exhibited enhanced activity in the presence of ΔP19RPR, suggesting that Eco-RnpA protein can effectively replace its Z. mobilis counterpart. Homologous and heterologous reconstituted enzymes in the presence of ΔP19RPR exhibited differences in their Km values and catalytic efficacies. Overall, the presence of the P19 stem points toward an adaption during the co-evolution of Zmo-RnpA and RPR that is essential for stabilizing the overall structure of the Z. mobilis RNase P. Finally, our results are in line with existing structural data on RNase P enzymes and provide biochemical support for the possible role of appended domains in RNase P RNA subunits.

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Section: ■ Discussionmentioning

confidence: 99%

On the Role of the Appended P19 Element in Type A RNAs of Bacterial RNase P

et al. 2014

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“…These protein subunits are designated Rpp14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, Rpp40, Pop1 and Pop5 (Figure 1). It remains unknown if human RNase P in different cell types or tissues has either distinct combinations of these ten Rpps or even a diverse composition due to recruitment of new proteins (49). Saccharomyces cerevisiae nuclear RNase P also possesses nine distinct protein subunits, all of which, except one, share human homologs (50).…”

Section: Eukaryal Rnase P: Large Rnps In Uni- and Multi-cellular Hostsmentioning

confidence: 99%

Archaeal/Eukaryal RNase P: subunits, functions and RNA diversification

Jarrous¹,

Gopalan²

2010

Nucleic Acids Research

106

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RNase P, a catalytic ribonucleoprotein (RNP), is best known for its role in precursor tRNA processing. Recent discoveries have revealed that eukaryal RNase P is also required for transcription and processing of select non-coding RNAs, thus enmeshing RNase P in an intricate network of machineries required for gene expression. Moreover, the RNase P RNA seems to have been subject to gene duplication, selection and divergence to generate two new catalytic RNPs, RNase MRP and MRP-TERT, which perform novel functions encompassing cell cycle control and stem cell biology. We present new evidence and perspectives on the functional diversification of the RNase P RNA to highlight it as a paradigm for the evolutionary plasticity that underlies the extant broad repertoire of catalytic and unexpected regulatory roles played by RNA-driven RNPs.

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“…In addition, the mutation exerts long-range effects, reducing the expression of the ND6 gene (encoding a subunit of complex I), which is co-transcribed with the eight tRNA genes of the mitochondrial light strand. On the heavy strand of the mtDNA, the mutation changes a stop codon of the MT-COI subunit of complex IV (cytochrome c oxidase) to a different stop codon(29)(30)(31)(32)(33)(158)(159)(160).…”

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Mitochondrial dysfunction: a neglected component of skin diseases

Feichtinger

Sperl

Bauer

et al. 2014

Experimental Dermatology

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Aberrant mitochondrial structure and function influence tissue homeostasis and thereby contribute to multiple human disorders and ageing. Ten per cent of patients with primary mitochondrial disorders present skin manifestations that can be categorized into hair abnormalities, rashes, pigmentation abnormalities and acrocyanosis. Less attention has been paid to the fact that several disorders of the skin are linked to alterations of mitochondrial energy metabolism. This review article summarizes the contribution of mitochondrial pathology to both common and rare skin diseases. We explore the intriguing observation that a wide array of skin disorders presents with primary or secondary mitochondrial pathology and that a variety of molecular defects can cause dysfunctional mitochondria. Among them are mutations in mitochondrial-and nuclear DNAencoded subunits and assembly factors of oxidative phosphorylation (OXPHOS) complexes; mutations in intermediate filament proteins involved in linking, moving and shaping of mitochondria; and disorders of mitochondrial DNA metabolism, fatty acid metabolism and heme synthesis. Thus, we assume that mitochondrial involvement is the rule rather than the exception in skin diseases. We conclude the article by discussing how improving mitochondrial function can be beneficial for aged skin and can be used as an adjunct therapy for certain skin disorders. Consideration of mitochondrial energy metabolism in the skin creates a new perspective for both dermatologists and experts in metabolic disease.Key words: energy metabolism -mitochondria -OXPHOS -respiratory chain -skin Accepted for publication 24 June 2014 Mitochondrial metabolism in the skinThe major function of mitochondria is to generate energy as ATP through oxidative phosphorylation (OXPHOS). In addition, mitochondria play important roles in heme synthesis, apoptosis and calcium homeostasis. In mitochondria, metabolites generated through breakdown of carbohydrates, proteins and fatty acids are fuelled into the citric acid cycle and OXPHOS to generate a proton gradient that is used to produce ATP via ATP synthase (complex V). Therefore, there are several levels at which defects can lead to diminished mitochondrial function and consequently to lower energy production.The OXPHOS system is composed of multisubunit respiratory chain complexes I-IV, the F 0 F 1 ATP synthase (complex V) and two electron carriers, coenzyme Q and cytochrome c. The subunits of the OXPHOS proteins are encoded by both mitochondrial and nuclear DNA. The mitochondrial DNA (mtDNA) contains genes for 13 OXPHOS polypeptides, 22 tRNAs and two ribosomal RNAs (1-3).Emerging evidence suggests that mitochondria are vital regulators of skin physiology. Mitochondrial metabolism regulates keratinocyte differentiation by producing mitochondrial reactive oxygen species (ROS), which are necessary to propagate the Notch and b-catenin signals that promote epidermal differentiation and hair follicle development, respectively (4). Interestingly, a recent study proposed...

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Partial purification and characterization of RNase P from human peripheral lymphocytes

Cited by 4 publications

References 17 publications

On the Role of the Appended P19 Element in Type A RNAs of Bacterial RNase P

On the Role of the Appended P19 Element in Type A RNAs of Bacterial RNase P

Archaeal/Eukaryal RNase P: subunits, functions and RNA diversification

Mitochondrial dysfunction: a neglected component of skin diseases

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