Qualitative and quantitative aspects of 2-5A synthesizing capacity of different marine sponges.
Identifieur interne : 002306 ( PubMed/Checkpoint ); précédent : 002305; suivant : 002307Qualitative and quantitative aspects of 2-5A synthesizing capacity of different marine sponges.
Auteurs : T Nu Reintamm [Estonie] ; Annika Lopp ; Anne Kuusksalu ; Juhan Subbi ; Merike KelveSource :
- Biomolecular engineering [ 1389-0344 ] ; 2003.
Descripteurs français
- KwdFr :
- 2',5'-Oligoadenylate synthetase (), 2',5'-Oligoadenylate synthetase (analyse), 2',5'-Oligoadenylate synthetase (biosynthèse), Activation enzymatique, Adénosine triphosphate (), Adénosine triphosphate (métabolisme), Animaux, Biologie marine (), Isoenzymes (), Isoenzymes (analyse), Isoenzymes (biosynthèse), Porifera (), Porifera (enzymologie), Spécificité d'espèce.
- MESH :
- analyse : 2',5'-Oligoadenylate synthetase, Isoenzymes.
- biosynthèse : 2',5'-Oligoadenylate synthetase, Isoenzymes.
- enzymologie : Porifera.
- métabolisme : Adénosine triphosphate.
- 2',5'-Oligoadenylate synthetase, Activation enzymatique, Adénosine triphosphate, Animaux, Biologie marine, Isoenzymes, Porifera, Spécificité d'espèce.
English descriptors
- KwdEn :
- 2',5'-Oligoadenylate Synthetase (analysis), 2',5'-Oligoadenylate Synthetase (biosynthesis), 2',5'-Oligoadenylate Synthetase (chemistry), Adenosine Triphosphate (chemistry), Adenosine Triphosphate (metabolism), Animals, Enzyme Activation, Isoenzymes (analysis), Isoenzymes (biosynthesis), Isoenzymes (chemistry), Marine Biology (methods), Porifera (classification), Porifera (enzymology), Species Specificity.
- MESH :
- chemical , analysis : 2',5'-Oligoadenylate Synthetase, Isoenzymes.
- chemical , biosynthesis : 2',5'-Oligoadenylate Synthetase, Isoenzymes.
- chemical , chemistry : 2',5'-Oligoadenylate Synthetase, Adenosine Triphosphate, Isoenzymes.
- chemical , metabolism : Adenosine Triphosphate.
- classification : Porifera.
- enzymology : Porifera.
- methods : Marine Biology.
- Animals, Enzyme Activation, Species Specificity.
Abstract
2-5A synthetase is an important component of the mammalian antiviral 2-5A system. At present, the existence of 2-5A synthetase in the lowest animals, the marine sponges, has been demonstrated, although this enzyme has not been found in bacteria, yeast or plants. Here, we studied the 2-5A synthesizing capacity and the product profile of a variety of marine sponges belonging to Demospongia subclasses Tetractinomorpha and Ceractinomorpha. The 2-5A synthetase activity varied largely, in the range of four orders of magnitude, depending on the sponge species. Compared with the enzymes of the mammalian 2-5A synthetase family, the most active sponge species exhibited a surprisingly high 2-5A synthetase specific activity. Unlike the mammalian 2-5A synthetases that produce 2-5A oligomers in the presence of a double-stranded RNA activator, the 2-5A synthetase(s) from sponges were active without the addition of dsRNA. The sponge species differed in their product profiles. A novel product pool formed by Chondrosia reniformis was identified as a series of long 2-5A oligomers (up to 17-mers) with the prevalence of heptamers and octamers. The large variability of qualitative and quantitative characteristics of sponge 2-5A synthetases may refer to the occurrence of a variety of 2-5A synthetase isozymes in sponges.
DOI: 10.1016/s1389-0344(03)00059-5
PubMed: 12919824
Affiliations:
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pubmed:12919824Le document en format XML
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<front><div type="abstract" xml:lang="en">2-5A synthetase is an important component of the mammalian antiviral 2-5A system. At present, the existence of 2-5A synthetase in the lowest animals, the marine sponges, has been demonstrated, although this enzyme has not been found in bacteria, yeast or plants. Here, we studied the 2-5A synthesizing capacity and the product profile of a variety of marine sponges belonging to Demospongia subclasses Tetractinomorpha and Ceractinomorpha. The 2-5A synthetase activity varied largely, in the range of four orders of magnitude, depending on the sponge species. Compared with the enzymes of the mammalian 2-5A synthetase family, the most active sponge species exhibited a surprisingly high 2-5A synthetase specific activity. Unlike the mammalian 2-5A synthetases that produce 2-5A oligomers in the presence of a double-stranded RNA activator, the 2-5A synthetase(s) from sponges were active without the addition of dsRNA. The sponge species differed in their product profiles. A novel product pool formed by Chondrosia reniformis was identified as a series of long 2-5A oligomers (up to 17-mers) with the prevalence of heptamers and octamers. The large variability of qualitative and quantitative characteristics of sponge 2-5A synthetases may refer to the occurrence of a variety of 2-5A synthetase isozymes in sponges.</div>
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<Abstract><AbstractText>2-5A synthetase is an important component of the mammalian antiviral 2-5A system. At present, the existence of 2-5A synthetase in the lowest animals, the marine sponges, has been demonstrated, although this enzyme has not been found in bacteria, yeast or plants. Here, we studied the 2-5A synthesizing capacity and the product profile of a variety of marine sponges belonging to Demospongia subclasses Tetractinomorpha and Ceractinomorpha. The 2-5A synthetase activity varied largely, in the range of four orders of magnitude, depending on the sponge species. Compared with the enzymes of the mammalian 2-5A synthetase family, the most active sponge species exhibited a surprisingly high 2-5A synthetase specific activity. Unlike the mammalian 2-5A synthetases that produce 2-5A oligomers in the presence of a double-stranded RNA activator, the 2-5A synthetase(s) from sponges were active without the addition of dsRNA. The sponge species differed in their product profiles. A novel product pool formed by Chondrosia reniformis was identified as a series of long 2-5A oligomers (up to 17-mers) with the prevalence of heptamers and octamers. The large variability of qualitative and quantitative characteristics of sponge 2-5A synthetases may refer to the occurrence of a variety of 2-5A synthetase isozymes in sponges.</AbstractText>
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