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Literature summary for 3.4.21.89 extracted from

  • Shipman-Roston, R.L.; Ruppel, N.J.; Damoc, C.; Phinney, B.S.; Inoue, K.
    The significance of protein maturation by plastidic type I signal peptidase 1 for thylakoid development in Arabidopsis chloroplasts (2010), Plant Physiol., 152, 1297-1308.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.89

Protein Variants

Protein Variants Comment Organism
additional information disruption of PLSP1 expression by a T-DNA insertion causes a seedling lethal phenotype in which development of internal membranes was severely retarded in cotyledon plastids. Construction of a plsp1-null mutant. Plastids that lack Plsp1 accumulate vesicles of variable sizes in the stroma, and they cause a reduction in accumulation of thylakoid proteins and that Plsp1 is involved in maturation of two additional lumenal proteins, OE23 and plastocyanin. OE33 associates with the stromal vesicles of the mutant plastids. Accumulation of improperly processed forms of Toc75 in the plastid envelope does not disrupt normal plant development, presence of posttranscriptional suppression of thylakoid protein accumulation in plsp1-1 plants, phenotype, overview Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast isozyme Plsp1 Arabidopsis thaliana 9507
-
thylakoid isozyme Plsp1 Arabidopsis thaliana 9579
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Synonyms

Synonyms Comment Organism
plastidic type I signal peptidase 1
-
 Arabidopsis thaliana
Plsp1
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
additional information proper maturation of lumenal proteins may be a key process for correct assembly of thylakoids Arabidopsis thaliana
physiological function Plsp1 is vital for proper thylakoid development in Arabidopsis thaliana chloroplasts. Plsp1 is also necessary for processing of an envelope protein, Toc75, and a thylakoid lumenal protein, OE33 Arabidopsis thaliana