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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)