Secretory ribonuclease genes and pseudogenes in true ruminants

Breukelman, Heleen J.; Munnik, N. van der; Kleineidam, RG; Furia, Adriana; Beintema, Jaap J.

doi:10.1016/s0378-1119(98)00177-2

Cited by 22 publications

(42 citation statements)

References 27 publications

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“…The percentages of conserved nucleotides in pairwise comparisons vary between 97% for the two toothed whale sequences and 76% for the ox A alpaca X pair. In accordance with the genes of most known expressed RNases 1 (Beintema et al 1988;Breukelman et al 1998), the alignment exhibits no indels except three deletions in the part coding for the Cterminal extension of bovine brain-type RNase. The camel RNase X sequence shares with the bovine pancreatic-type and most other RNase genes the stop codon at nt positions 373-375 that is not present in ruminant brain-type sequences, thereby causing extended proteins.…”

Section: Rnase Sequencessupporting

confidence: 53%

“…The oligonucleotide B/SP, 5Ј-GGGGATCCGGGTCCAGCCTTC-CCTGGG-3Ј, corresponding to the C-terminal part of the signal peptide of bovine secretory RNases with an added BamHI site (boldfaced) was used as forward primer (Breukelman et al 1998). It was combined with either the threefold degenerated primer E2A, 5Ј-GGGAATTCGAAG/ CCATCA/GAAGTGG/CACTGG-3Ј, corresponding to amino acids 117 to 123 or the primer ErumAS, degenerated at only one position, 5Ј-GGGAATTCAGGCAGATGCCTTTGTGATGAAGC/TGG-3Ј (Eurosequence BV, Groningen), annealing to a region 33 to 58 nucleotides downstream of the stop codon of the ruminant pancreatic and seminal but not brain-type ribonuclease genes (Breukelman et al 1998). The latter two primers introduced EcoRI sites (boldfaced) in the PCR products.…”

Section: Methodsmentioning

confidence: 99%

“…Phylogenetic analysis were performed with the nucleotide positions 1 to 348 of the sequences described in this article and the homologous pancreatic and brain-type RNase genes of ox (Bos taurus) Sasso et al 1991) and hog deer (Axis porcinus) (Breukelman et al 1998) but excluding the less well-established alpaca sequence. RNase sequences of mouse (Mus musculus) (Samuelson et al 1991), Chinese hamster (Cricetulus longicaudatus), and human (Homo sapiens) (Haugg and Schein 1992) were used as outgroup.…”

Section: Phylogenetic Analysesmentioning

confidence: 99%

“…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: 96%

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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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Section: Rnase Sequencessupporting

confidence: 53%

Section: Methodsmentioning

confidence: 99%

Section: Phylogenetic Analysesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

See 2 more Smart Citations

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

et al. 1999

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“…These two genes are the result of gene duplication that occurred before the radiation of ruminants at least 35 MY ago. In all other ruminants, the seminal ribonuclease gene either contains deleterious mutations or is not expressed [28][29][30], which suggests that the seminal ribonuclease gene had been a pseudogene for much of its history, but was revived recently in the cow. How this could have happened is unclear.…”

Section: Pseudogenizationmentioning

confidence: 99%

Evolution by gene duplication: an update

Zhang

2003

Trends in Ecology & Evolution

1,922

1,586

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Human endothelial cells selectively express large amounts of pancreatic‐type ribonuclease (RNase 1)

Landré

Hewett

Olivot

et al. 2002

J of Cellular Biochemistry

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Pyrimidine-specific ribonucleases are a superfamily of structurally related enzymes with distinct catalytic and biological properties. We used a combination of enzymatic and non-enzymatic assays to investigate the release of such enzymes by isolated cells in serum-free and serum-containing media. We found that human endothelial cells typically expressed large amounts of a pancreatic-type RNase that is related to, if not identical to, human pancreatic RNase. This enzyme exhibits pyrimidine-specific catalytic activity, with a marked preference for poly(C) substrate over poly(U) substrate. It was potently inhibited by placental RNase inhibitor, the selective pancreatic-type RNase inhibitor Inhibit-Ace, and a polyclonal antibody against human pancreatic RNase. The enzyme isolated from medium conditioned by immortalized umbilical vein endothelial cells (EA.hy926) possesses an amino-terminal sequence identical to that of pancreatic RNase, and shows molecular heterogeneity (molecular weights 18,000-26,000) due to different degrees of N-glycosylation. Endothelial cells from arteries, veins, and capillaries secreted up to 100 ng of this RNase daily per million cells, whereas levels were low or undetectable in media conditioned by other cell types examined. The corresponding messenger RNA was detected by RT-PCR in most cell types tested so far, and level of its expression was in keeping with the amounts of protein. The selective strong release of pancreatic-type RNase by endothelial cells suggests that it is endowed with non-digestive functions and involved in vascular homeostasis.

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Secretory ribonuclease genes and pseudogenes in true ruminants

Cited by 22 publications

References 27 publications

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

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

Evolution by gene duplication: an update

Human endothelial cells selectively express large amounts of pancreatic‐type ribonuclease (RNase 1)

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