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Biochimica et biophysica acta1981; 654(1); 77-85; doi: 10.1016/0005-2787(81)90138-6

Nucleic acid-protein interactions. Degradation of double-stranded RNA by glycosylated ribonucleases.

Abstract: 1. Extensively glycosylated ribonucleases, like the enzymes from pig and horse pancreas, show a much higher activity on double-stranded RNAs than similarly charged, carbohydrate-free RNAases under stranded assay conditions (relatively high salt concentrations). Glycosylated pig and horse pancreas RNAases also show a larger destabilizing effect on double-stranded poly[d(A-T)] X poly[d(A-T)], than that displayed by bovine RNAase A under these conditions. Both activities show a similar dependence on the ionic strength of the medium. 2. A partial enzymic removal of the heterosaccharide side chains from pig and horse RNAases reduces but their degradative activity on double-stranded RNA and their destabilizing action on poly[d(A-T)] X poly[d(A-T)]. 3. These results are tentatively correlated with a modification of the microenvironment of the enzyme protein caused by its extensive glycosylation.
Publication Date: 1981-06-26 PubMed ID: 7272311DOI: 10.1016/0005-2787(81)90138-6Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research paper explores how glycosylated ribonucleases, specifically from pig and horse pancreas, cause degradation of double-stranded RNA more effectively than non-glycosylated versions. It also delves into how the removal of heterosaccharide side chains from these glycosylated ribonucleases can affect their degradative activities and destabilizing effects.

Findings on Glycosylated Ribonucleases and their Degradative Abilities

  • The researchers found that extensively glycosylated ribonucleases, from both pig and horse pancreas, had greater degradative effects on double stranded RNAs (or dsRNA) compared to ribonucleases that were carbohydrate-free.
  • Under high salt concentration conditions, these glycosylated ribonucleases demonstrated more pronounced destabilizing effects on double-stranded poly[d(A-T)] X poly[d(A-T)], a specific DNA/RNA duplex, than the non-glycosylated equivalent derived from the bovine.
  • The dependency of these activities on the ionic strength of the medium was found to be similar.

Consequences of Enzymic Removal of Heterosaccharide Side Chains

  • It was observed that a partial enzymic removal of the heterosaccharide side chains from pig and horse ribonucleases dampened their degradative activity on double-stranded RNA. This also lessened their destabilizing action on poly[d(A-T)] X poly[d(A-T)].

Proposed Correlation

  • The findings were proposed to be potentially a result of changes to the microenvironment of the protein enzyme due to its extensive glycosylation, altering its behaviour and interaction with double-stranded RNA. This correlation, however, is a tentative conclusion that requires further validation.

Cite This Article

APA
Carsana A, Furia A, Gallo A, Beintema JJ, Libonati M. (1981). Nucleic acid-protein interactions. Degradation of double-stranded RNA by glycosylated ribonucleases. Biochim Biophys Acta, 654(1), 77-85. https://doi.org/10.1016/0005-2787(81)90138-6

Publication

ISSN: 0006-3002
NlmUniqueID: 0217513
Country: Netherlands
Language: English
Volume: 654
Issue: 1
Pages: 77-85

Researcher Affiliations

Carsana, A
    Furia, A
      Gallo, A
        Beintema, J J
          Libonati, M

            MeSH Terms

            • Animals
            • Carbohydrates / analysis
            • Cattle
            • Cricetinae
            • Glycoproteins / metabolism
            • Guinea Pigs
            • Horses
            • Nucleic Acid Denaturation
            • Pancreas / enzymology
            • Poly dA-dT
            • RNA, Double-Stranded
            • Ribonucleases / metabolism
            • Species Specificity
            • Substrate Specificity
            • Swine

            Citations

            This article has been cited 1 times.
            1. Libonati M, Sorrentino S. Revisiting the action of bovine ribonuclease A and pancreatic-type ribonucleases on double-stranded RNA. Mol Cell Biochem 1992 Nov 18;117(2):139-51.
              doi: 10.1007/BF00230753pubmed: 1488047google scholar: lookup