| Autor: |
Callahan, F.E., Ghirardi, M.L., Sopory, S.K., Mehta, A.M., Edelman, M., Mattoo, A.K. |
| Zdroj: |
Journal of Biological Chemistry; September 1990, Vol. 265 Issue: 26 p15357-15360, 4p |
| Abstrakt: |
Two forms of the 32 kDa-D1 reaction center protein of photosystem II (PSII), having slightly different mobilities on denaturing polyacrylamide gels, have been resolved in Spirodela oligorrhiza, Glycine max L., Gossypium hirsutum L., Triticum aestivum L., and Zea mays L. The protein band with faster mobility is identified as the 32 kDa-D1 protein, and the less mobile band as a novel form, designated 32*. The two forms are structurally similar based on immunological and partial proteolytic tests. 32* is associated exclusively with the grana and is present in the PSII reaction center. Temporally, 32* appears several hours after the translocation of newly synthesized and processed 32 kDa-D1 protein from the stroma lamellae to the grana. Formation of the 32* is strictly light-dependent under physiological light intensities and correlates with a reciprocal loss of the 32-kDa form. Light induced formation of 32* is inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea but is not coupled to linear electron transport. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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