Molecular cloning of the gene encoding the bovine brain ribonucelase and its expression in different regions of the brain

Sasso, Maurizio; Carsana, Antonella; Confalone, Elena; Cosi, Cristina; Sorrentino, Salvatore; Viola, Maria Pia; Palmieri, Marta; Russo, E.; Furia, Adriana

doi:10.1093/nar/19.23.6469

Cited by 44 publications

(28 citation statements)

References 26 publications

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“…Moreover, only preliminary studies had been performed on isolated enzyme (44,45). To enable relevant comparisons, we also analyzed well known homologs: human RNase 1, bovine RNase A, and both monomeric (mBSR) and dimeric (dBSR) forms of BSR.…”

Section: Resultsmentioning

confidence: 99%

“…A second perplexity surrounds BRB: what is the purpose of its extended, hydrophobic C-terminal tail? Although all ruminant brain ribonucleases possess a similar tail, the amino acid sequences of these regions are not conserved, and seem to have arisen through multiple substitutions and deletions (19,44). The tail is known to be O-glycosylated at two sites (25), but the significance of these oligosaccharide chains is not known.…”

Section: Discussionmentioning

confidence: 99%

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Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Eller

Lomax

Raines

2014

Journal of Biological Chemistry

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Background: RNase 1 is an RNA-degrading enzyme conserved in mammals and with unknown biological function. Results: RNase 1 homologs in human and cow display different biochemical and biological properties, implying divergent physiology. Conclusion: Bovine brain ribonuclease, not RNase A, is the functional homolog of human RNase 1. Significance: Fundamental insight into the biology and evolution of human RNase 1 is attained from analyses of homologous proteins.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Eller

Lomax

Raines

2014

Journal of Biological Chemistry

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“…Three strictly homologous enzymes have been found in different tissues of the bovine species; in fact, while pancreatic ribonuclease (Richards and Wyckoff 1971;Blackburn and Moore 1982) is produced in the pancreas and to a lesser extent in other tissues, a seminal ribonuclease is synthesized in seminal vesicles and secreted in the seminal fluid (D'Alessio et al 1972;Furia et al 1983;Suzuki et al 1987), and a brain ribonuclease is synthesized in the central nervous system (Watanabe et al 1988;Sasso et al 1991). Despite the high degree of identity of their primary structures, each enzyme is endowed with specific structural features.…”

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confidence: 99%

“…The brain ribonuclease (BRb RNAase) is a monomer of 141 amino acids, with an oligosaccharide chain linked to the asparagine residue 62. This protein bears a carboxy-terminal extension relative to the pancreatic and seminal enzymes, in which the two polar amino acid residues, Thr 129 and Ser 133, have covalently bound carbohydrates (Watanabe et al 1988;Sasso et al 1991). These features of the brain and seminal enzymes have never been found in the homologous proteins isolated from pancreatic tissues.…”

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confidence: 99%

Sequences related to the ox pancreatic ribonuclease coding region in the genomic DNA of mammalian species

Beintema

Confalone

et al. 1993

J Mol Evol

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Mammalian pancreatic ribonucleases form a family of homologous proteins that has been extensively investigated. The primary structures of these enzymes were used to derive phylogenetic trees. These analyses indicate that the presence of three strictly homologous enzymes in the bovine species (the pancreatic, seminal, and cerebral ribonucleases) is due to gene duplication events which occurred during the evolution of ancestral ruminants. In this paper we present evidence that confirms this finding and that suggests an overall structural conservation of the putative ribonuclease genes in ruminant species. We could also demonstrate that the sequences related to ox ribonuclease coding regions present in genomic DNA of the giraffe species are the orthologues of the bovine genes encoding the three ribonucleases mentioned above.

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“…At present, this superfamily includes at least four distinct sequence lineages (Riordan and D'Alessio 1997) and two species-limited clusters (Palmieri et al 1985;Watanabe et al 1988;Sasso et al 1991;Batten et al 1997;Larson et al 1997), as well as the two most rapidly evolving functional coding sequences known among primates (Rosen berg et al 1995). The basis for this remarkable expenditure of evolutionary energy remains uncertain.…”

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confidence: 99%

Ribonuclease k6: Chromosomal Mapping and Divergent Rates of Evolution within the RNase A Gene Superfamily

Deming¹,

Dyer²,

Bankier³

et al. 1998

Genome Res.

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We have localized the gene encoding human RNase k6 to within ∼120 kb on the long (q) arm of chromosome 14 by HAPPY mapping. With this information, the relative positions of the six human RNase A ribonucleases that have been mapped to this locus can be inferred. To further our understanding of the individual lineages comprising the RNase A superfamily, we have isolated and characterized 10 novel genes orthologous to that encoding human RNase k6 from Great Ape, Old World, and New World monkey genomes. Each gene encodes a complete ORF with no less than 86% amino acid sequence identity to human RNase k6 with the eight cysteines and catalytic histidines (H 15 and H 123 ) and lysine (K 38 ) typically observed among members of the RNase A superfamily. Interesting trends include an unusually low number of synonymous substitutions (K s ) observed among the New World monkey RNase k6 genes. When considering nonsilent mutations, RNase k6 is a relatively stable lineage, with a nonsynonymous substitution rate of 0.40 × 10 −9 nonsynonymous substitutions/ nonsynonymous site/year (ns/ns/yr). These results stand in contrast to those determined for the primate orthologs of the two closely related ribonucleases, the eosinophil-derived neurotoxin (EDN) and eosinophil cationic protein (ECP), which have incorporated nonsilent mutations at very rapid rates (1.9 × 10 −9 and 2.0 × 10 −9 ns/ns/yr, respectively). The uneventful trends observed for RNase k6 serve to spotlight the unique nature of EDN and ECP and the unusual evolutionary constraints to which these two ribonuclease genes must be responding.[The sequence data described in this paper have been submitted to the GenBank data library under accession nos. AF037081-AF037090.]Ribonuclease k6 (RNase k6) is a recently identified member of the RNase A superfamily, a group of otherwise divergent proteins defined by specific elements of sequence homology to the prototype, Ribonuclease A. In previous work we have shown that human RNase k6 is encoded by a single-copy gene, with mRNA transcripts expressed in numerous somatic tissues (Rosenberg and Dyer 1996). Within this superfamily, RNase k6 is most closely related to the two eosinophil ribonucleases, the eosinophilderived neurotoxin (EDN/RNase 2) and eosinophil cationic protein (ECP/RNase 3), although mRNA encoding RNase k6 was detected in peripheral blood neutrophils and monocytes, but not eosinophils. From an enzymatic perspective, recombinant RNase k6 was found to be a relatively efficient ribonuclease, with catalytic activity only ∼40-fold lower than that of recombinant EDN (Rosenberg andDyer 1995a, 1996); in contrast, the catalytic actvity of recombinant ECP was found to be ∼2000-fold lower than that of recombinant EDN (Rosenberg and Dyer 1997).The RNase A superfamily has been the subject of numerous studies that have elucidated patterns of evolution at the molecular level (Beintema et al. 1986Benner and Allemann 1989;Fitch and Beintema 1990;Confalone et al. 1995;Jermann et al. 1995;Rosenberg et al. 1995;Trabesinger-Ruef et al. 1996...

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Molecular cloning of the gene encoding the bovine brain ribonucelase and its expression in different regions of the brain

Cited by 44 publications

References 26 publications

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Sequences related to the ox pancreatic ribonuclease coding region in the genomic DNA of mammalian species

Ribonuclease k6: Chromosomal Mapping and Divergent Rates of Evolution within the RNase A Gene Superfamily

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