Identification of a wheat germ agglutinin-sensitive ATPase in yeast nuclei.
We have found that wheat germ agglutinin (WGA), a lectin that specifically binds to N-acetylglucosamine residues inhibits the in vitro transport of plasmid DNA, pJDB219, into yeast nuclei. Histochemical staining of the isolated nuclei with biotinylated WGA and streptavidin-biotinylated peroxidase complex revealed the presence of WGA-binding materials around the nuclear pore under an electron microscope. Using WGA-agarose column chromatography of yeast nuclear extracts, a novel Mg2+-dependent ATPase was isolated. Its activity was highly sensitive to WGA and stimulated by Nonidet P-40 or phosphatidylserine. We suggest that the WGA-sensitive ATPase plays a role in yeast nuclear transport of DNA.
Tsuchiya
E
E
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
Hiraga
K
K
Fukui
S
S
Miyakawa
T
T
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002467:Cell Nucleus / Q000201:enzymology; D002853:Chromatography, Liquid; D011975:Receptors, Mitogen / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014162:Transfection; D014909:Wheat Germ Agglutinins / Q000494:pharmacology*
D011975:Receptors, Mitogen; D014909:Wheat Germ Agglutinins; C027503:wheat germ agglutinin receptor; D000251:Adenosine Triphosphatases