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Literature summary for 3.1.13.4 extracted from

  • Baggs, J.E.; Green, C.B.
    Nocturnin, a deadenylase in Xenopus laevis retina a mechanism for posttranscriptional control of circadian-related mRNA (2003), Curr. Biol., 13, 189-198 .
    View publication on PubMed
Search for more literature for 3.1.13.4

Cloned(Commentary)

Cloned (Comment) Organism
-
 Xenopus laevis
expression in Escherichia coli BL21 (DE3) Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Xenopus laevis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm nocturnin is expressed in the cytoplasm of rod and cone photoreceptor cells Xenopus laevis 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ nocturnin nuclease activity is magnesium dependent Xenopus laevis

Organism

Organism UniProt Comment Textmining
Xenopus laevis P79942
-
-
Xenopus laevis Q90ZA1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Xenopus laevis

Source Tissue

Source Tissue Comment Organism Textmining
photoreceptor cell expression of nocturnin mRNA is confined to the clock-containing photoreceptor cell layer within the retina Xenopus laevis
-
retina
-
 Xenopus laevis
-
retina constitutively present in most retinal cell Xenopus laevis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mRNA-poly(A) + H2O nocturnin removes the poly(A) tail from a synthetic RNA substrate in a process known as deadenylation. It specifically degrades the 3' poly(A) tail Xenopus laevis ?
-
 ?
mRNA-poly(A) + H2O
-
 Xenopus laevis 5'-AMP + ?
-
 ?

Synonyms

Synonyms Comment Organism
PARN
-
 Xenopus laevis

Expression

Organism Comment Expression
Xenopus laevis nocturnin is rhythmically expressed in the cytoplasm of the retinal retina photoreceptor cells, with peak mRNA levels in the early night up

General Information

General Information Comment Organism
physiological function while nocturnin is rhythmically expressed in the cytoplasm of the retinal photoreceptor cells, the only other described vertebrate deadenylase, PARN, is constitutively present in most retinal cells, including the photoreceptors. The distinct spatial and temporal expression of nocturnin and PARN suggests that there may be specific mRNA targets of each deadenylase Xenopus laevis
physiological function while nocturnin is rhythmically expressed in the cytoplasm of the retinal photoreceptor cells, the only other described vertebrate deadenylase, PARN, is constitutively present in most retinal cells, including the photoreceptors. The distinct spatial and temporal expression of nocturnin and PARN suggests that there may be specific mRNA targets of each deadenylase. Since deadenylation regulates mRNA decay and/or translational silencing, it is proposed that nocturnin deadenylates clock-related transcripts in a novel mechanism for posttranscriptional regulation in the circadian clock or its outputs Xenopus laevis