Molecular evolution of genes encoding ribonucleases in ruminant species

Confalone, Elena; Beintema, Jj; Sasso, Maurizio; Carsana, Antonella; Palmieri, Marta; Vento, MT; Furia, Adriana

doi:10.1007/bf00173164

Cited by 27 publications

(33 citation statements)

References 24 publications

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“…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%

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: 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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“…This tree includes two homologous sequences expressed in bovine brain and seminal vesicles besides that of the pancreatic enzyme. Orthologous genes of these three RNases were identified in giraffe, sheep, hog deer, and roe deer but not in species outside the suborder Ruminantia (Breukelman et al 1993(Breukelman et al , 1998Confalone et al 1995). Therefore, they probably derive from two gene duplications in an ancestor of the ruminants.…”

Section: Introductionmentioning

confidence: 94%

Inclusion of Cetaceans Within the Order Artiodactyla Based on Phylogenetic Analysis of Pancreatic Ribonuclease Genes

et al. 1999

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Mammalian secretory ribonucleases (RNases 1) form a family of extensively studied homologous proteins that were already used for phylogenetic analyses at the protein sequence level previously. In this paper we report the determination of six ribonuclease gene sequences of Artiodactyla and two of Cetacea. These sequences have been used with ruminant homologues in phylogenetic analyses that supported a group including hippopotamus and toothed whales, a group of ruminant pancreatic and brain-type ribonucleases, and a group of tylopod sequences containing the Arabian camel pancreatic ribonuclease gene and Arabian and Bactrian camel and alpaca RNase 1 genes of unknown function. In all analyses the pig was the first diverging artiodactyl. This DNA-based tree is compatible to published trees derived from a number of other genes. The differences to those trees obtained with ribonuclease protein sequences can be explained by the influence of convergence of pancreatic RNases from hippopotamus, camel, and ruminants and by taking into account the information from third codon positions in the DNA-based analyses. The evolution of sequence features of ribonucleases such as the distribution of positively charged amino acids and of potential glycosylation sites is described with regard to increased double-stranded RNA cleavage that is observed in several cetacean and artiodactyl RNases which may have no role in ruminant or ruminant-like digestion.

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“…This is the most known for any given species. Thus, no other species, other than ruminants, possess the seminal and brain enzymes (Breukelman et al, 1993;Confalone et al, 1995;Trabesinger-Ruef et al, 1996), and bovine angiogenin-2 may also be similarly limited. This evolutionary multiplication of genes may require new specificities for the expressed genes, or a new environment for exercising existing functions, or perhaps even new functions.…”

Section: Comparison Of Bovine Angiogenin-2 and Other Proteinsmentioning

confidence: 99%

An Angiogenic Protein from Bovine Serum and Milk — Purification and Primary Structure of Angiogenin‐2

Strydom

Bond

Vallée

1997

European Journal of Biochemistry

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Bovine serum and milk contain a basic angiogenic protein that binds tightly to placental ribonuclease inhibitor. It was purified from both sources by ion-exchange and reversed-phase chromatographies. Its amino acid sequence revealed that it is a member of the ribonuclease superfamily. It contains 123 amino acids in a single polypeptide chain, is cross-linked by three disulfide bonds, is glycosylated at Asn33, and is 57 % identical to bovine angiogenin. The amino-terminal and carboxyl-terminal residues are pyroglutamic acid and proline, respectively. The protein has ribonucleolytic activity that is similar to, but somewhat lower than, that of bovine angiogenin, i.e. very low relative to RNase. It is angiogenically potent on chicken chorioallantoic membrane, but less so than angiogenin. The sequence and activities demonstrate that this protein is a second, distinct, member of the angiogenin sub-family of pancreatic ribonucleases, and is referred to as angiogenin-2.

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Molecular evolution of genes encoding ribonucleases in ruminant species

Cited by 27 publications

References 24 publications

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Inclusion of Cetaceans Within the Order Artiodactyla Based on Phylogenetic Analysis of Pancreatic Ribonuclease Genes

An Angiogenic Protein from Bovine Serum and Milk — Purification and Primary Structure of Angiogenin‐2

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