Literature summary for 3.1.13.4 extracted from

Nilsson, P.; Henriksson, N.; Niedzwiecka, A.; Balatsos, N.A.; Kokkoris, K.; Eriksson, J.; Virtanen, A.
A multifunctional RNA recognition motif in poly(A)-specific ribonuclease with cap and poly(A) binding properties (2007), J. Biol. Chem., 282, 32902-32911.

Search for more literature for 3.1.13.4

Application

Application	Comment	Organism
additional information	RRM motif of PARN harbors both poly(A) and cap binding properties, RRM plays an important role in PARN activity, i.e. recognition and dependence on both the cap structure and poly(A) tail during poly(A) hydrolysis. Trp475 plays an essential role in PARN cap recognition, whereas Glu455 and especially Trp456 play auxiliary roles. Cap binding is not essential for the hydrolytic activity of PARN. Cap and RNA-binding sites of the RRM are structurally and functionally separated from each other	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
DNA fragment corresponding to amino acids 443-560 in the human PARN sequence cloned into pCR 2.1TOPO vector and subsequently subcloned into the pET19b vector, recombinant PARN or PARN mutants expressed in Escherichia coli strain BL21(DE3)	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E455/W456/W475A	severely defective in cap binding, active deadenylase	Homo sapiens
E455A	no defect in its cap binding	Homo sapiens
additional information	PARN(443-560/W456/W475A) mutant is severely defective in cap binding, has RNA binding properties	Homo sapiens
W456A	cap binding slightly affected	Homo sapiens
W475A	severely defective in cap binding	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by metal affinity resin	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
poly(A) RNA + H2O	the RRM of PARN binds RNA	Homo sapiens	5'-AMP + ?	-	?

Synonyms

Synonyms	Comment	Organism
PARN	-	Homo sapiens

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Release 2023.1 (January 2023)