In general, they all contain
tightly bound nucleotides and their physiological functions
are controlled by the exchange of tightly bound nucleotide
contents of the complexes. We plan to elucidate the
molecular mechanism of individual systems and, on the
other hand, to unravel the general principles behind
their regulation. Currently, we are studying the regulation
of retinal cGMP cascade in phototransduction, the enzymology
of chloroplast and mitochondrial FoF1 proton ATPase,
recA and DNA gyrase. A detailed structural and functional
comparison of these enzymes may help us to understand
their common evolutionary path.
Selected Publications:
Yamada, M., Ho, Y-K., Lee, R.H., Kontani, K., Takahashill,
K., Katadall, T. and Kurachi, Y. (1994): "Muscarinic
K+ channels are activated by a subunits and inhibited
by the GDP-bound form of a ý subunit of transducin."
Biochem. Biophys. Res. Comm. 200, 1484-1490.
Tar, A., Ting, T.D. and Ho, Y-K. (1994): "Purification
of bovine retinal cGMP phosphodiesterase", Methods
of Enzymology, Vol. "G-Proteins", Iyengar,
R., ed., pp 3-12, Academic Press, New York.
Morrison, D.F., Ting, T.D., Vallury, V., Ho, Y-K., Crouch,
R.K., Corson, D.W., Mangini, N.J. and Pepperberg, D.R.
(1995): "Reduced light-dependent phosphorylation
of an analog visual pigment containing 9-demethylretinal
as its chromophore". J. Biol. Chem. 270, 6718-6721.
Oh, U., Ho, Y-K. and Kim, D. (1995): "Modulation
of the Serotonin-activated K+ channel by G protein subunits
and nucleotides in rat hippocampal neurons". J.
Membrane Biology 147, 241-253. |
