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- W3165237215 abstract "FtsH metalloproteases found in eubacteria, animals, and plants are well-known for their vital role in the maintenance and proteolysis of membrane proteins. Their location is restricted to organelles of endosymbiotic origin, the chloroplasts, and mitochondria. In the model organism Arabidopsis thaliana, there are 17 membrane-bound FtsH proteases containing an AAA+ (ATPase associated with various cellular activities) and a Zn2+ metalloprotease domain. However, in five of those, the zinc-binding motif HEXXH is either mutated (FtsHi1, 2, 4, 5) or completely missing (FtsHi3), rendering these enzymes presumably inactive in proteolysis. Still, homozygous null mutants of the pseudo-proteases FtsHi1, 2, 4, 5 are embryo-lethal. Homozygous ftshi3 or a weak point mutant in FTSHi1 are affected in overall plant growth and development. This review will focus on the findings concerning the FtsHi pseudo-proteases and their involvement in protein import, leading to consequences in embryogenesis, seed growth, chloroplast, and leaf development and oxidative stress management." @default.
- W3165237215 created "2021-06-07" @default.
- W3165237215 creator A5040823337 @default.
- W3165237215 creator A5080570208 @default.
- W3165237215 date "2021-05-31" @default.
- W3165237215 modified "2023-09-25" @default.
- W3165237215 title "The FtsHi Enzymes of Arabidopsis thaliana: Pseudo-Proteases with an Important Function" @default.
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- W3165237215 doi "https://doi.org/10.3390/ijms22115917" @default.
- W3165237215 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8197885" @default.
- W3165237215 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34072887" @default.
- W3165237215 hasPublicationYear "2021" @default.
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