A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish

Pizzo, Elio; Merlino, Antonello; Turano, Mimmo; Krauss, Irene Russo; Coscia, Francesca; Varcamonti, Mario; Furia, Adriana; Giancola, Concetta; Mazzarella, L.; Sica, F.; D’Alessio, Giuseppe

doi:10.1042/bj20100892

Cited by 26 publications

(23 citation statements)

References 49 publications

(97 reference statements)

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“…The gene encoding anole RNase 1 (Gene ID: 100555482) was amplified from Anoliscarolinensis liver cDNA and inserted into pET22b. The gene encoding zebrafish RNase 3/4[51,52] (Gene ID: 100101462) was amplified from Danio rerio cDNA and inserted into pET22b. The program Signal P was used to predict and exclude peptide leader sequences for all proteins.…”

Section: Methodsmentioning

confidence: 99%

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

Lomax

Bianchetti

Chang

et al. 2014

Journal of Molecular Biology

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Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the existence of a non-mammalian RI has been uncertain. Here, we report on the identification and characterization of RI homologs from chicken and anole lizard. These proteins bind to RNases from multiple species, but exhibit much greater affinity for their cognate RNases than for mammalian RNases. To reveal the basis for this differential affinity, we determined the crystal structure of mouse, bovine, and chicken RI·RNase complexes to a resolution of 2.20, 2.21, and 1.92 Å, respectively. A combination of structural, computational, and bioinformatic analyses enabled the identification of two residues that appear to contribute to the differential affinity for RNases. We also found marked differences in oxidative instability between mammalian and non-mammalian RIs, indicating evolution toward greater oxygen-sensitivity in RIs from mammalian species. Taken together, our results illuminate the structural and functional evolution of RI, along with its dynamic role in vertebrate biology.

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Section: Methodsmentioning

confidence: 99%

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

Lomax

Bianchetti

Chang

et al. 2014

Journal of Molecular Biology

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“…The RNaseA superfamily is a vertebrate-specific gene family that comprises a wide set of secreted ribonucleases displaying a variety of biological properties [ 1 , 2 ]. In particular, distant related members were reported to share innate immunity properties, suggesting that the vertebrate RNases have evolved as a host-defense family [ 3 , 4 , 5 ]. Eight functional members are found in humans, known as the “canonical RNases” ( Figure 1 ), sharing a common structural fold and catalytic triad [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation

Pulido

Arranz-Trullén

Prats-Ejarque

et al. 2016

IJMS

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Human Ribonuclease 6 is a secreted protein belonging to the ribonuclease A (RNaseA) superfamily, a vertebrate specific family suggested to arise with an ancestral host defense role. Tissue distribution analysis revealed its expression in innate cell types, showing abundance in monocytes and neutrophils. Recent evidence of induction of the protein expression by bacterial infection suggested an antipathogen function in vivo. In our laboratory, the antimicrobial properties of the protein have been evaluated against Gram-negative and Gram-positive species and its mechanism of action was characterized using a membrane model. Interestingly, our results indicate that RNase6, as previously reported for RNase3, is able to specifically agglutinate Gram-negative bacteria as a main trait of its antimicrobial activity. Moreover, a side by side comparative analysis with the RN6(1–45) derived peptide highlights that the antimicrobial activity is mostly retained at the protein N-terminus. Further work by site directed mutagenesis and structural analysis has identified two residues involved in the protein antimicrobial action (Trp1 and Ile13) that are essential for the cell agglutination properties. This is the first structure-functional characterization of RNase6 antimicrobial properties, supporting its contribution to the infection focus clearance.

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“…For example, the mouse ( Mus musculus ) has more than 20 (Rosenberg et al 2001; Nitto et al 2005, 2006; Pizzo et al 2006, 2008, 2011; Cho and Zhang 2007; Tao et al 2011). Using the RNases identified in the six mammalian genomes, including human, mouse, rat, cow, dog, and opossum, Cho and Zhang (2006) previously determined that the expansion of the RNase A superfamily occurred in the common ancestor of these six mammals before the divergence of the marsupial and the placental mammals (∼190 Ma).…”

Section: Introductionmentioning

confidence: 99%

The Expansion and Functional Diversification of the Mammalian Ribonuclease A Superfamily Epitomizes the Efficiency of Multigene Families at Generating Biological Novelty

Goo

Cho

2013

Genome Biology and Evolution

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The ribonuclease (RNase) A superfamily is a vertebrate-specific gene family. Because of a massive expansion that occurred during the early mammalian evolution, extant mammals in general have much more RNase genes than nonmammalian vertebrates. Mammalian RNases have been associated with diverse physiological functions including digestion, cytotoxicity, angiogenesis, male reproduction, and host defense. However, it is still uncertain when their expansion occurred and how a wide array of functions arose during their evolution. To answer these questions, we generate a compendium of all RNase genes identified in 20 complete mammalian genomes including the platypus, Ornithorhynchus anatinus. Using this, we delineate 13 ancient RNase gene lineages that arose before the divergence between the monotreme and the other mammals (∼220 Ma). These 13 ancient gene lineages are differentially retained in the 20 mammals, and the rate of protein sequence evolution is highly variable among them, which suggest that they have undergone extensive functional diversification. In addition, we identify 22 episodes of recent expansion of RNase genes, many of which have signatures of adaptive functional differentiation. Exemplifying this, bursts of gene duplication occurred for the RNase1, RNase4, and RNase5 genes of the little brown bat (Myotis lucifugus), which might have contributed to the species’ effective defense against heavier pathogen loads caused by its communal roosting behavior. Our study illustrates how host-defense systems can generate new functions efficiently by employing a multigene family, which is crucial for a host organism to adapt to its ever-changing pathogen environment.

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A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish

Cited by 26 publications

References 49 publications

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles

Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation

The Expansion and Functional Diversification of the Mammalian Ribonuclease A Superfamily Epitomizes the Efficiency of Multigene Families at Generating Biological Novelty

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