Human PARN peptide

Name: Human PARN peptide
SKU: DAG-P1019
Rating: 5 (1 reviews)

Synthetic Human PARN peptide

COA

SDS

Datasheet

Summary

Specificity

Ubiquitous.

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

Belongs to the CAF1 family.Contains 1 R3H domain.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Entrez Gene ID

5073

Antigen Description

The protein encoded by this gene is a 3-exoribonuclease, with similarity to the RNase D family of 3-exonucleases. It prefers poly(A) as the substrate, hence, efficiently degrades poly(A) tails of mRNAs. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. This protein is also involved in silencing of certain maternal mRNAs during oocyte maturation and early embryonic development, as well as in nonsense-mediated decay (NMD) of mRNAs that contain premature stop codons. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]

Function

mRNA 3-UTR binding; metal ion binding; nuclease activity; nucleotide binding; poly(A) RNA binding; poly(A)-specific ribonuclease activity; protein binding; protein kinase binding;

Synonyms

PARN; poly(A)-specific ribonuclease; DAN; poly(A)-specific ribonuclease PARN; deadenylating nuclease; deadenylation nuclease; polyadenylate-specific ribonuclease; poly(A)-specific ribonuclease (deadenylation nuclease);

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Effect of magnesium ions on the thermal stability of human poly(A)-specific ribonuclease

FEBS LETTERS

Authors: Liu, Wei-Feng; Zhang, Ao; Cheng, Yuan; Zhou, Hai-Meng; Yan, Yong-Bin

Abstract

Poly(A)-specific ribonuclease (PARN), a member of the DEDD family, is a key enzyme involved in the deadenylation of mRNA in higher eukaryotic cells. In this research, it was found that Mg2+ could protect PARN against thermal inactivation by increasing the midpoint of inactivation and decreasing the inactivation rate. This protective effect was unique to Mg2+ in a concentration-dependent manner. However, the thermal unfolding and aggregation was promoted by the addition of Mg2+ at high temperatures. These results revealed that Mg2+ might have dual effects on PARN stability: protecting the active site but endangering the overall structural stability. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Poly(A)-specific ribonuclease regulates the processing of small-subunit rRNAs in human cells

NUCLEIC ACIDS RESEARCH

Authors: Ishikawa, Hideaki; Yoshikawa, Harunori; Izumikawa, Keiichi; Miura, Yutaka; Taoka, Masato; Nobe, Yuko; Yamauchi, Yoshio; Nakayama, Hiroshi; Simpson, Richard J.; Isobe, Toshiaki; Takahashi, Nobuhiro

Abstract

Ribosome biogenesis occurs successively in the nucleolus, nucleoplasm, and cytoplasm. Maturation of the ribosomal small subunit is completed in the cytoplasm by incorporation of a particular class of ribosomal proteins and final cleavage of 18S-E prerRNA (18S-E). Here, we show that poly(A)-specific ribonuclease (PARN) participates in steps leading to 18S-E maturation in human cells. We found PARN as a novel component of the pre-40S particle pulled down with the pre-ribosome factor LTV1 or Bystin. Reverse pull-down analysis revealed that PARN is a constitutive component of the Bystin-associated pre-40S particle. Knockdown of PARN or exogenous expression of an enzyme-dead PARN mutant (D28A) accumulated 18S-E in both the cytoplasm and nucleus. Moreover, expression of D28A accumulated 18S-E in Bystin-associated pre-40S particles, suggesting that the enzymatic activity of PARN is necessary for the release of 18S-E from Bystin-associated pre-40S particles. Finally, RNase H-based fragmentation analysis and 3'-sequence analysis of 18S-E species present in cells expressing wild-type PARN or D28A suggested that PARN degrades the extended regions encompassing nucleotides 5-44 at the 3' end of mature 18S rRNA. Our results reveal a novel role for PARN in ribosome biogenesis in human cells.