Chromium(III) .beta.,.gamma.-bidentate guanine nucleotide complexes as probes of the GTP-activated cGMP cascade of retinal rod outer segments

Biochemistry ◽  
1988 ◽  
Vol 27 (21) ◽  
pp. 8209-8218 ◽  
Author(s):  
Suzanne E. Frey ◽  
Vijay N. Hingorani ◽  
Saiu Mei Su-Tsai ◽  
Yee Kin Ho
Keyword(s):  
Rod Outer Segments ◽  
Guanine Nucleotide ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments

scholarly journals Inhibition of the GTPase activity of transducin by an NAD+:arginine ADP-ribosyltransferase from turkey erythrocytes

1987 ◽  
Vol 248 (3) ◽  
pp. 749-754 ◽  
Author(s):  
P A Watkins ◽  
Y Kanaho ◽  
J Moss
Keyword(s):  
Nucleotide Binding ◽  
Rod Outer Segments ◽  
Guanine Nucleotide ◽  
Gtpase Activity ◽  
Adp Ribosylation ◽  
Outer Segments ◽  
Retinal Rod ◽  
Guanine Nucleotide Binding ◽  
Adp Ribosyltransferase ◽  
Retinal Rod Outer Segments

The bacterial toxins, choleragen and pertussis toxin, inhibit the light-stimulated GTPase activity of bovine retinal rod outer segments by catalysing the ADP-ribosylation of the alpha-subunit (T alpha) of transducin [Abood, Hurley, Pappone, Bourne & Stryer (1982) J. Biol. Chem. 257, 10540-10543; Van Dop, Yamanaka, Steinberg, Sekura, Manclark, Stryer & Bourne (1984) J. Biol. Chem. 259, 23-26]. Incubation of retinal rod outer segments with NAD+ and a purified NAD+:arginine ADP-ribosyltransferase from turkey erythrocytes resulted in approx. 60% inhibition of GTPase activity. Inhibition was dependent on both enzyme and NAD+, and was potentiated by the non-hydrolysable GTP analogues guanosine 5′-[beta gamma-imido]triphosphate (p[NH]ppG) and guanosine 5′-[beta gamma-methylene]triphosphate (p[CH2]ppG). The transferase ADP-ribosylated both the T alpha and T beta subunits of purified transducin. T alpha (39 kDa), after ADP-ribosylation, migrated as two distinct peptides with molecular masses of 42 kDa and 46 kDa on SDS/polyacrylamide-gel electrophoresis. T beta (36 kDa), after ADP-ribosylation, migrated as a 38 kDa peptide. With purified transducin subunits, it was observed that the GTPase activity of ADP-ribosylated T alpha, reconstituted with unmodified T beta gamma and photolysed rhodopsin, was decreased by 80%; conversely, reconstitution of T alpha with ADP-ribosyl-T beta gamma resulted in only a 19% inhibition of GTPase. Thus ADP-ribosylation of T alpha, the transducin subunit that contains the guanine nucleotide-binding site, has more dramatic effects on GTPase activity than does modification of the critical ‘helper subunits’ T beta gamma. To elucidate the mechanism of GTPase inhibition by transferase, we studied the effect of ADP-ribosylation on p[NH]pp[3H]G binding to transducin. It was shown previously that modification of transducin by choleragen, which like transferase ADP-ribosylates arginine residues, did not affect guanine nucleotide binding. ADP-ribosylation by the transferase, however, decreased p[NH]pp[3H]G binding, consistent with the hypothesis that choleragen and transferase inhibit GTPase by different mechanisms.

scholarly journals Mg2+ -ATP induces filament growth from retinal rod outer segments with disrupted plasma membranes

FEBS Letters ◽  
1987 ◽  
Vol 211 (1) ◽  
pp. 35-40 ◽  
Author(s):  
K.R. Parker ◽  
L.E. Schaechter ◽  
J.W. Lewis ◽  
K.L. Zeman ◽  
D.S. Kliger ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments

Patterns of Experimental Allergic Uveitis Induced by Rhodopsin and Retinal Rod Outer Segments

1980 ◽  
Vol 12 (3) ◽  
pp. 165-176 ◽  
Author(s):  
George E. Marak, Jr ◽  
Hitoshi Shichi ◽  
Narsing A. Rao ◽  
Waldon B. Wacker
Keyword(s):  
Rod Outer Segments ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments ◽  
Experimental Allergic

Effect of tocopherol and taurine on membrane fluidity of retinal rod outer segments

1987 ◽  
Vol 45 (6) ◽  
pp. 769-776 ◽  
Author(s):  
Julio Moran ◽  
Patricia Salazar ◽  
Herminia Pasantes-Morales
Keyword(s):  
Membrane Fluidity ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments

Purification of a complex of transducin βγ subunits from isotonic extracts of bovine retinal rod outer segments

BIOPHYSICS ◽  
2010 ◽  
Vol 55 (6) ◽  
pp. 908-910 ◽  
Author(s):  
D. N. Orlov ◽  
T. G. Orlova ◽  
A. R. Nezvetsky ◽  
N. Ya. Orlov
Keyword(s):  
Rod Outer Segments ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments
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