Abstract
| Language | English |
|---|---|
| Pages | 2095-2105 |
| Number of pages | 11 |
| Journal | Biochemical Journal |
| Volume | 474 |
| Issue number | 12 |
| DOIs | |
| State | Published - 2017 |
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1-N-histidine phosphorylation of ChlD by the AAA⁺ ChlI2 stimulates magnesium chelatase activity in chlorophyll synthesis. / Sawicki, Artur; Shuaixiang, Zhou; Kwiatkowski, Kathrin; Luo, Meizhong; Willows, Robert.
In: Biochemical Journal, Vol. 474, No. 12, 2017, p. 2095-2105.Research output: Contribution to journal › Article
TY - JOUR
T1 - 1-N-histidine phosphorylation of ChlD by the AAA⁺ ChlI2 stimulates magnesium chelatase activity in chlorophyll synthesis
AU - Sawicki,Artur
AU - Shuaixiang,Zhou
AU - Kwiatkowski,Kathrin
AU - Luo,Meizhong
AU - Willows,Robert
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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.
U2 - 10.1042/BCJ20161094
DO - 10.1042/BCJ20161094
M3 - Article
VL - 474
SP - 2095
EP - 2105
JO - Biochemical Journal
T2 - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 12
ER -