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Literature summary for 2.7.7.8 extracted from

  • Germain, A.; Herlich, S.; Larom, S.; Kim, S.H.; Schuster, G.; Stern, D.B.
    Mutational analysis of Arabidopsis chloroplast polynucleotide phosphorylase reveals roles for both RNase PH core domains in polyadenylation, RNA 3'-end maturation and intron degradation (2011), Plant J., 67, 381-394.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D625N naturally occuring mutation in the catalytic site, inactive mutant Arabidopsis thaliana
G596R naturally occuring mutation near the catalytic domain, inactive mutant. Mutant G596R fails to fold correctly, perhaps as a consequence of its inability to bind phosphate, and is thus marked for degradation Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Arabidopsis thaliana 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana polynucleotide phosphorylase is an exoribonuclease ?
-
?
additional information Arabidopsis thaliana Col-0. polynucleotide phosphorylase is an exoribonuclease ?
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Arabidopsis thaliana Col-0.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information polynucleotide phosphorylase is an exoribonuclease Arabidopsis thaliana ?
-
?
additional information polynucleotide phosphorylase is an exoribonuclease Arabidopsis thaliana Col-0. ?
-
?

Synonyms

Synonyms Comment Organism
chloroplast PNPase
-
Arabidopsis thaliana
cpPNPase
-
Arabidopsis thaliana
RNase PH
-
Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction enzyme depletion decreases splicing efficiency and inhibits intron degradation, effects on intron metabolism, overview. In mutants lacking cpPNPase activity, unusual RNA patterns occur, intron-containing fragments also accumulate in mutants. Mutants show gene-dependent and intermediate RNA phenotypes, suggesting that reduced enzyme activity differentially affects chloroplast transcripts Arabidopsis thaliana
additional information also see for EC 2.7.7.56. RNase PH, EC 2.7.7.8, consists of tandem N-terminal RNase PH-like segments, known as core domains, as well as KH and S1 RNA-binding domains. The conserved residue D625 is located in the catalytic site and functions in phosphorolysis Arabidopsis thaliana
physiological function the chloroplastidic enzyme has a major role in maturing mRNA and rRNA 3'-ends, but also participates in RNA degradation through exonucleolytic digestion and polyadenylation.Cchloroplast PNPase and a poly(A) polymerase share the polymerization role in wild-type plants. Chloroplast PNPase appears to be required for a degradation step following endonucleolytic cleavage of the excised lariat. The enzyme functions depend absolutely on the catalytic site within the second duplicated RNase PH domain, and appear to be modulated by the first RNase PH domain, but both PNPase domains contribute to chloroplast rRNA and mRNA processing, overview Arabidopsis thaliana