Abstract
Isolated chloroplast coupling factor (CF1), when depleted of its ɛ‐subunit, has a high ATPase activity which can be inhibited by binding ɛ to a single high‐affinity (K d = 1.4 × 10−10 M) site. In CF1 reduced by dithiothreitol (DTT), however, ɛ at this binding site is no longer inhibitory. Instead, 3 equivalent, lower affinity (K d = 6 × 10−8 M), inhibitory binding sites for ɛ are observed, whether or not the high‐affinity site contains a bound ɛ‐subunit. Binding of ɛ to the high‐affinity site protects CF1 against trypsin activation, while binding to the low‐affinity site does not, showing that occupation of each class of site has a different effect on CF1 structure. The effects of DTT can be interpreted in terms of a reduction in intersubunit cooperativity in CF1.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:45 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 1:29 a.m.) |
Indexed | 1 year, 11 months ago (Sept. 17, 2023, 12:56 a.m.) |
Issued | 37 years, 2 months ago (June 20, 1988) |
Published | 37 years, 2 months ago (June 20, 1988) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 37 years, 2 months ago (June 20, 1988) |
@article{Andralojc_1988, title={Two distinct types of ɛ‐binding site exist in chloroplast coupling factor (CF1)}, volume={233}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(88)80471-x}, DOI={10.1016/0014-5793(88)80471-x}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Andralojc, P.J. and Harris, D.A.}, year={1988}, month=jun, pages={403–407} }