Literature summary extracted from
Wang, F.; Qi, Y.; Malnoe, A.; Choquet, Y.; Wollman, F.A.; de Vitry, C.
The high light response and redox control of thylakoid FtsH protease in Chlamydomonas reinhardtii (2017), Mol. Plant, 10, 99-114 .
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
3.4.24.B20 |
thylakoid |
- |
Chlamydomonas reinhardtii |
9579 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.B20 |
Chlamydomonas reinhardtii |
A8IL08 and A8J6C7 |
A8IL08 i.e. isoform FtsH1, A8J6C7 i.e. isoform FtsH2 |
- |
Expression
EC Number |
Organism |
Comment |
Expression |
---|
3.4.24.B20 |
Chlamydomonas reinhardtii |
mRNA levels of isoforms Ftsh1 and Ftsh increase upon high light exposure |
up |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.24.B20 |
physiological function |
upon high light exposure, the FtsH1 and FtsH2 and subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in modest upregulation of FtsH1/2 proteins. High light increases the protease activity through a redox-controlled reduction of intermolecular disulfide bridges. In a FTSH1 promoter-deficient mutant, the abundance of FtsH1 and FtsH2 proteins are loosely coupled (decreased by 70% and 30%, respectively) with no formation of large and stable homo-oligomers. High light tolerance is tightly correlated with the abundance of the FtsH protease |
Chlamydomonas reinhardtii |