Cloning and Sequencing of a cDNA Clone Encoding the Photosystem I PsaD Subunit from Chlamydomonas reinhardtii
نویسندگان
چکیده
منابع مشابه
A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas reinhardtii.
FNR (EC 1.18.1.2) is a flavoenzyme that plays an important role in the metabolism of photosynthetic organisms. FNR catalyzes the final step of the linear photosynthetic electron transfer chain by mediating the passage of electrons from reduced Fd to NADP+. FNR is situated at a branch point in electron flow, playing a key role in regulating the relative amounts of cyclic and noncyclic electron f...
متن کاملA Nucleus-Encoded Chloroplast Phosphoprotein Governs Expression of the Photosystem I Subunit PsaC in Chlamydomonas reinhardtii.
The nucleo-cytoplasmic compartment exerts anterograde control on chloroplast gene expression through numerous proteins that intervene at posttranscriptional steps. Here, we show that the maturation of psaC mutant (mac1) of Chlamydomonas reinhardtii is defective in photosystem I and fails to accumulate psaC mRNA. The MAC1 locus encodes a member of the Half-A-Tetratricopeptide (HAT) family of sup...
متن کاملThe PsaD Subunit of Photosystem I ' Mutations in the Basic Domain Reduce the Leve 1 of PsaD in the Membranes
Fd. PsaD and PsaE facilitate Fd docking, and PsaE may be The PsaD subunit of photosystem I (PSI) i s a peripheral protein involved in cyclic electron flow "nd PSI (Chimis, 1996). that provides a docking site for ferredoxin and interacts with the PsaD is a crucial component on the reducing side of PSI. PsaB, PsaC, and PsaL subunits of PSI. We used site-directed muThe insertional inactivation of ...
متن کاملThe PsaD subunit of photosystem I. Mutations in the basic domain reduce the level of PsaD in the membranes.
The PsaD subunit of photosystem I (PSI) is a peripheral protein that provides a docking site for ferredoxin and interacts with the PsaB, PsaC, and PsaL subunits of PSI. We used site-directed mutagenesis to determine the function of a basic region in PsaD of the cyanobacterium Synechocystis sp. PCC 6803. We generated five mutant strains in which one or more charged residues were altered. Western...
متن کاملNucleotide sequence of a cDNA encoding the chloroplast sedoheptulose-1,7-bisphosphatase from Chlamydomonas reinhardtii.
SBPase is an enzyme of the reductive pentose-P pathway that catalyzes the hydrolytic cleavage of Pi from the C-1 position of sedoheptulose-1,7-bisP. Together with Fru-1,6bisphosphatase it occupies a strategically important position in the pathway and has been shown to contribute to the fine control of the Calvin cycle (Schimkat et al., 1990). SBPase seems to be a highly regulated enzyme. It not...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 1995
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.107.4.1485