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The carboxyl-terminal extension of the D1 protein of photosystem II is not required for optimal photosynthetic performance under CO2- and light-saturated growth conditions
Year:
1992
Source of publication :
Journal of Biological Chemistry
Authors :
Lers, Amnon
;
.
Volume :
267
Co-Authors:
Lers, A., Department of Zoology, Duke University, Durham, NC 27706, United States
Heifetz, P.B., Department of Botany, Duke University, Durham, NC 27706, United States
Boynton, J.E., Department of Botany, Duke University, Durham, NC 27706, United States
Gillham, N.W., Department of Zoology, Duke University, Durham, NC 27706, United States
Osmond, C.B., Department of Botany, Duke University, Durham, NC 27706, United States, Res. School of Biological Sciences, Australian National University, Canberra, ACT 2601, Australia
Facilitators :
From page:
17494
To page:
17497
(
Total pages:
4
)
Abstract:
Synthesis of the photosystem II D1 protein as a precursor with a carboxyl-terminal extension occurs in almost all eukaryotic photosynthetic organisms examined so far, as well as in cyanobacteria. Processing of the D1 precursor has been recently postulated to play a regulatory role in the light-dependent migration of photosystem II units from the unstacked to the stacked thylakoids (Bowyer, J. M., Packer, J. C. L., McCormack, B. A., Whitelegge, J. P., Robinson, C., and Taylor, M. A. (1992) J. Biol. Chem. 267, 5424-5433). To test this hypothesis, site-directed mutagenesis and chloroplast transformation have been used to create a "preprocessed" mutant Chlamydomonas strain which synthesizes mature D1 protein directly. We have found that this strain is indistinguishable from wild type in terms of photosynthetic performance and cell doubling time under CO2- and light-saturated photoautotrophic growth conditions.
Note:
Related Files :
Animal
carboxy terminal sequence
Chlamydomonas
DNA
light
photosynthesis
plant growth
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More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29592
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:48
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Scientific Publication
The carboxyl-terminal extension of the D1 protein of photosystem II is not required for optimal photosynthetic performance under CO2- and light-saturated growth conditions
267
Lers, A., Department of Zoology, Duke University, Durham, NC 27706, United States
Heifetz, P.B., Department of Botany, Duke University, Durham, NC 27706, United States
Boynton, J.E., Department of Botany, Duke University, Durham, NC 27706, United States
Gillham, N.W., Department of Zoology, Duke University, Durham, NC 27706, United States
Osmond, C.B., Department of Botany, Duke University, Durham, NC 27706, United States, Res. School of Biological Sciences, Australian National University, Canberra, ACT 2601, Australia
The carboxyl-terminal extension of the D1 protein of photosystem II is not required for optimal photosynthetic performance under CO2- and light-saturated growth conditions
Synthesis of the photosystem II D1 protein as a precursor with a carboxyl-terminal extension occurs in almost all eukaryotic photosynthetic organisms examined so far, as well as in cyanobacteria. Processing of the D1 precursor has been recently postulated to play a regulatory role in the light-dependent migration of photosystem II units from the unstacked to the stacked thylakoids (Bowyer, J. M., Packer, J. C. L., McCormack, B. A., Whitelegge, J. P., Robinson, C., and Taylor, M. A. (1992) J. Biol. Chem. 267, 5424-5433). To test this hypothesis, site-directed mutagenesis and chloroplast transformation have been used to create a "preprocessed" mutant Chlamydomonas strain which synthesizes mature D1 protein directly. We have found that this strain is indistinguishable from wild type in terms of photosynthetic performance and cell doubling time under CO2- and light-saturated photoautotrophic growth conditions.
Scientific Publication
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