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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Arabidopsis thaliana | 9507 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Arabidopsis thaliana Col-0. | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Arabidopsis thaliana | - |
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 | Comment | Organism |
---|---|---|
chloroplast PNPase | - |
Arabidopsis thaliana |
cpPNPase | - |
Arabidopsis thaliana |
RNase PH | - |
Arabidopsis thaliana |
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 |