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Literature summary for 3.4.21.53 extracted from

  • Smakowska, E.; Czarna, M.; Janska, H.
    Mitochondrial ATP-dependent proteases in protection against accumulation of carbonylated proteins (2014), Mitochondrion, 19, 245-251.
    View publication on PubMed
Search for more literature for 3.4.21.53

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial matrix
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 Arabidopsis thaliana 5759
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
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seed
-
 Arabidopsis thaliana
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Subunits

Subunits Comment Organism
More the enzyme has two domains: the N-terminal ATPase domain with chaperone-like properties and the C-terminal proteolytic domain specific for the ATP-dependent protease family Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
i-AAA Protease
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 Arabidopsis thaliana
lon
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 Arabidopsis thaliana
lon protease
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 Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
ATP a ofmitochondrial ATP-dependent protease Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism plant mitochondrial protein carbonylation, an irreversible oxidative protein modification that inactivates the protein function, and role of the ATP-dependent proteases in defending mitochondria against accumulation of carbonylated proteins, overview. In plants, carbonylated proteins are found in virtually all cellular compartments - cytosol, chloroplasts, peroxisomes, nucleus, and mitochondria - and in the entire plant life cycle with especially high levels at certain stages of growth and development. Carbonylated breakdown products of mitochondrial proteins might act as secondary messengers in retrograde signaling from plant mitochondria to the nucleus. mitochondria depend on a series of pathways that continuously monitor and remove oxidatively damaged proteins Arabidopsis thaliana
physiological function the Lon protease is an ATP-dependent serine protease recognized as a key protease up-regulated under oxidative stress and involved in the removal of oxidized proteins, the mitochondrial inner membrane i-AAA protease is a crucial component of the defense against accumulation of carbonylated proteins. Due to the irreversible and unrepairable nature of protein carbonylation, proteolytic elimination of oxidatively damaged polypeptides is the major process of the mitochondrial protein quality control system under oxidative stress as first line of defense Arabidopsis thaliana