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Regulation of trehalase expression inhibits apoptosis in diapause cysts of Artemia.
- Source :
-
The Biochemical journal [Biochem J] 2013 Dec 01; Vol. 456 (2), pp. 185-94. - Publication Year :
- 2013
-
Abstract
- Trehalase, which specifically hydrolyses trehalose into glucose, plays an important role in the metabolism of trehalose. Large amounts of trehalose are stored in the diapause encysted embryos (cysts) of Artemia, which are not only vital to their extraordinary stress resistance, but also provide a source of energy for development after diapause is terminated. In the present study, a mechanism for the transcriptional regulation of trehalase was described in Artemia parthenogenetica. A trehalase-associated protein (ArTAP) was identified in Artemia-producing diapause cysts. ArTAP was found to be expressed only in diapause-destined embryos. Further analyses revealed that ArTAP can bind to a specific intronic segment of a trehalase gene. Knockdown of ArTAP by RNAi resulted in the release of cysts with coarse shells in which two chitin-binding proteins were missing. Western blotting showed that the level of trehalase was increased and apoptosis was induced in these ArTAP-knockdown cysts compared with controls. Taken together, these results show that ArTAP is a key regulator of trehalase expression which, in turn, plays an important role in trehalose metabolism during the formation of diapause cysts.
- Subjects :
- Animals
Artemia cytology
Artemia embryology
Arthropod Proteins genetics
Base Sequence
Cloning, Molecular
DNA-Binding Proteins physiology
Embryo, Nonmammalian cytology
Gene Expression Regulation, Enzymologic
Introns
Molecular Sequence Data
Protein Binding
Protein Transport
Sequence Analysis, DNA
Transcription, Genetic
Trehalose genetics
Apoptosis
Artemia enzymology
Arthropod Proteins metabolism
Embryo, Nonmammalian enzymology
Trehalose metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1470-8728
- Volume :
- 456
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 24063546
- Full Text :
- https://doi.org/10.1042/BJ20131020