S-Adenosyl-L-homocysteine hydrolase is sequestered into actin rods in Dictyostelium discoideum spores.
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.
Kishi
Y
Y
Electron Microscopy Center, The Tokyo Metropolitan Institute of Medical Science, Tokyo Metropolitan Organization for Medical Research, Japan.
Sugo
T
T
Mahadeo
D
D
Cotter
D
D
Sameshima
M
M
D000199:Actins / Q000378:metabolism*; D043383:Adenosylhomocysteinase; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003599:Cytoskeleton / Q000201:enzymology* / Q000648:ultrastructure; D004023:Dictyostelium / Q000201:enzymology* / Q000502:physiology / Q000648:ultrastructure; D006867:Hydrolases / Q000737:chemistry / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013170:Spores / Q000201:enzymology / Q000502:physiology / Q000648:ultrastructure
D000199:Actins; D011993:Recombinant Fusion Proteins; D019000:Phosphotyrosine; D006867:Hydrolases; D043383:Adenosylhomocysteinase