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Literature summary for 3.6.4.13 extracted from

  • Asakura, Y.; Galarneau, E.; Watkins, K.P.; Barkan, A.; van Wijk, K.J.
    Chloroplast RH3 DEAD box RNA helicases in maize and Arabidopsis function in splicing of specific group II introns and affect chloroplast ribosome biogenesis (2012), Plant Physiol., 159, 961-974.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis Arabidopsis thaliana
phylogenetic analysis Zea mays

Protein Variants

Protein Variants Comment Organism
additional information construction of double knockdown mutant rh3-4/clpr2-1, chloroplast rps12-int1 splicing defects in mutant rh3-4 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Arabidopsis thaliana 9507
-
chloroplast stroma as well as thylakoid membranes Zea mays 9507
-
chloroplast stroma
-
Zea mays 9570
-
additional information enzyme RH3 accumulates in stroma and nucleoids of green tissues, with peak accumulation during chloroplast biogenesis Arabidopsis thaliana
-
-
additional information ZmRH3 associates with 50S preribosome particles as well as nucleoids. Enzyme RH3 accumulates in stroma and nucleoids of green tissues, with peak accumulation during chloroplast biogenesis Zea mays
-
-
thylakoid membrane
-
Zea mays 42651
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8L7S8
-
-
Zea mays A0A1D6GDY8 ZmRH3A
-

Source Tissue

Source Tissue Comment Organism Textmining
flower
-
Arabidopsis thaliana
-
leaf AtRH3 is predominantly expressed in young leaves, peaking in 2-week-old seedlings and decreasing to very low levels in older leaf tissue Arabidopsis thaliana
-
leaf the enzyme abundance is high in the sink-source transition zone of developing maize leaves, coincident with the plastid biogenesis machinery Zea mays
-
additional information enzyme RH3 accumulates in stroma and nucleoids of green tissues, with peak accumulation during chloroplast biogenesis Zea mays
-
additional information enzyme RH3 accumulates in stroma and nucleoids of green tissues, with peak accumulation during chloroplast biogenesis. No enzyme activity in stems or roots of seedlings Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-
silique
-
Arabidopsis thaliana
-

Subunits

Subunits Comment Organism
More domain organization of RH3 protein Arabidopsis thaliana
More domain organization of RH3 protein Zea mays

Synonyms

Synonyms Comment Organism
AtRH3
-
Arabidopsis thaliana
DEAD box RNA helicase
-
Arabidopsis thaliana
DEAD box RNA helicase
-
Zea mays
ZmRH3
-
Zea mays
ZmRH3A
-
Zea mays
ZmRH3B
-
Zea mays

Expression

Organism Comment Expression
Arabidopsis thaliana 5 to 10fold upregulation of enzyme AtRH3 in plastid caseinolytic protease mutants. AtRH3 up-regulation is not a direct consequence of reduced proteolysis but constitutes a compensatory response at both RH3 transcript and protein levels to impaired chloroplast biogenesis. RH3 up-regulation is nt specific for ClpPR core protease mutants but is a general result of defects in chloroplast biogenesis up

General Information

General Information Comment Organism
malfunction AtRH3 null mutants are embryo lethal, whereas a weak allele results in pale-green seedlings with defects in splicing of several group II introns and rRNA maturation as well as reduced levels of assembled ribosomes,phenotype overview Arabidopsis thaliana
additional information domain organization of RH3 protein Zea mays
additional information domain organization of RH3 protein. RH3 and ClpR2 interact genetically, but RH3 is unlikely to be a substrate for the Clp protease Arabidopsis thaliana
physiological function the enzyme is under strong developmental control, and its abundance sharply peaks in the sink-source transition zone of developing maize leaves, coincident with the plastid biogenesis machinery Zea mays
physiological function the enzyme is under strong developmental control. Cross talk between the chloroplast and the nucleus is used to regulate RH3 levels. Enzyme RH3 functions in the splicing of group II introns and possibly also contributes to the assembly of the 50S ribosomal particle Arabidopsis thaliana