scholarly journals Mg chelatase in chlorophyll synthesis and retrograde signaling inChlamydomonas reinhardtii: CHLI2 cannot substitute for CHLI1

2016 ◽  
Vol 67 (13) ◽  
pp. 3925-3938 ◽  
Author(s):  
Pawel Brzezowski ◽  
Marina N. Sharifi ◽  
Rachel M. Dent ◽  
Marius K. Morhard ◽  
Krishna K. Niyogi ◽  
...  
2005 ◽  
Vol 4 (2) ◽  
pp. 253-261 ◽  
Author(s):  
Tudor Borza ◽  
Cristina E. Popescu ◽  
Robert W. Lee

ABSTRACT The presence of plastids in diverse eukaryotic lineages that have lost the capacity for photosynthesis is well documented. The metabolic functions of such organelles, however, are poorly understood except in the case of the apicoplast in the Apicomplexa, a group of intracellular parasites including Plasmodium falciparum, and the plastid of the green alga Helicosporidium sp., a parasite for which the only host-free stage identified in nature so far is represented by cysts. As a first step in the reconstruction of plastid functions in a nonphotosynthetic, predominantly free-living organism, we searched for expressed sequence tags (ESTs) that correspond to nucleus-encoded plastid-targeted polypeptides in the green alga Prototheca wickerhamii. From 3,856 ESTs, we found that 71 unique sequences (235 ESTs) correspond to different nucleus-encoded putatively plastid-targeted polypeptides. The identified proteins predict that carbohydrate, amino acid, lipid, tetrapyrrole, and isoprenoid metabolism as well as de novo purine biosynthesis and oxidoreductive processes take place in the plastid of P. wickerhamii. Mg-protoporphyrin accumulation and, therefore, plastid-to-nucleus signaling might also occur in this nonphotosynthetic organism, as we identified a transcript which encodes subunit I of Mg-chelatase, the enzyme which catalyzes the first committed step in chlorophyll synthesis. Our data indicate a far more complex metabolism in P. wickerhamii's plastid compared with the metabolic pathways predicted to be located in the apicoplast of P. falciparum and the plastid of Helicosporidium sp.


2017 ◽  
Vol 474 (12) ◽  
pp. 2095-2105 ◽  
Author(s):  
Artur Sawicki ◽  
Shuaixiang Zhou ◽  
Kathrin Kwiatkowski ◽  
Meizhong Luo ◽  
Robert D. Willows

Magnesium chelatase (Mg-chelatase) inserts magnesium into protoporphyrin during the biosynthesis of chlorophyll and bacteriochlorophyll. Enzyme activity is reconstituted by forming two separate preactivated complexes consisting of a GUN4/ChlH/protoporphyrin IX substrate complex and a ChlI/ChlD enzyme ‘motor’ complex. Formation of the ChlI/ChlD complex in both Chlamydomonas reinhardtii and Oryza sativa is accompanied by phosphorylation of ChlD by ChlI, but the orthologous protein complex from Rhodobacter capsulatus, BchI/BchD, gives no detectable phosphorylation of BchD. Phosphorylation produces a 1-N-phospho-histidine within ChlD. Proteomic analysis indicates that phosphorylation occurs at a conserved His residue in the C-terminal integrin I domain of ChlD. Comparative analysis of the ChlD phosphorylation with enzyme activities of various ChlI/ChlD complexes correlates the phosphorylation by ChlI2 with stimulation of Mg-chelatase activity. Mutation of the H641 of CrChlD to E641 prevents both phosphorylation and stimulation of Mg-chelatase activity, confirming that phosphorylation at H641 stimulates Mg-chelatase. The properties of ChlI2 compared with ChlI1 of Chlamydomonas and with ChlI of Oryza, shows that ChlI2 has a regulatory role in Chlamydomonas.


2006 ◽  
Vol 62 (3) ◽  
pp. 325-337 ◽  
Author(s):  
Haitao Zhang ◽  
Jinjie Li ◽  
Jeong-Hoon Yoo ◽  
Soo-Cheul Yoo ◽  
Sung-Hwan Cho ◽  
...  

2019 ◽  
Vol 45 (3) ◽  
pp. 460 ◽  
Author(s):  
Ning HE ◽  
Xue-Yang WANG ◽  
Liang-Zi CAO ◽  
Da-Wei CAO ◽  
Yu LUO ◽  
...  

Crop Science ◽  
1979 ◽  
Vol 19 (2) ◽  
pp. 261-264 ◽  
Author(s):  
T. Gulya ◽  
J. M. Dunleavy

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