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S-Adenosyl-L-homocysteine hydrolase is sequestered into actin rods in Dictyostelium discoideum spores.
- Source :
-
FEBS letters [FEBS Lett] 2001 Nov 23; Vol. 508 (3), pp. 433-7. - Publication Year :
- 2001
-
Abstract
- Here we show evidence that S-adenosyl-L-homocysteine hydrolase (SAHH) is linked to the actin cytoskeleton. Actin rods formed in Dictyostelium discoideum spores during the final stage of development are structurally composed of novel bundles of actin filaments. SAHH only accumulates with actin at this stage of development in the life cycle of D. discoideum. Recently SAHH is believed to be a target for antiviral chemotherapy and the suppression of T cells. Our finding may contribute to designing novel antiviral and immunosuppressive drugs.
- Subjects :
- Adenosylhomocysteinase
Amino Acid Sequence
Animals
Chromatography, High Pressure Liquid
Cytoskeleton ultrastructure
Dictyostelium physiology
Dictyostelium ultrastructure
Hydrolases chemistry
Microscopy, Electron
Molecular Sequence Data
Phosphorylation
Phosphotyrosine metabolism
Recombinant Fusion Proteins metabolism
Spores enzymology
Spores physiology
Spores ultrastructure
Actins metabolism
Cytoskeleton enzymology
Dictyostelium enzymology
Hydrolases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 508
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 11728467
- Full Text :
- https://doi.org/10.1016/s0014-5793(01)03105-2