Abstract
PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p-Pop2p-Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 533-539 |
| Number of pages | 7 |
| Journal | Nature Structural and Molecular Biology |
| Volume | 13 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 26 2006 |
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PUF proteins bind Pop2p to regulate messenger RNAs. / Goldstrohm, Aaron C.; Hook, Brad A.; Seay, Daniel J.; Wickens, Marvin.
In: Nature Structural and Molecular Biology, Vol. 13, No. 6, 26.06.2006, p. 533-539.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - PUF proteins bind Pop2p to regulate messenger RNAs
AU - Goldstrohm, Aaron C.
AU - Hook, Brad A.
AU - Seay, Daniel J.
AU - Wickens, Marvin
PY - 2006/6/26
Y1 - 2006/6/26
N2 - PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p-Pop2p-Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.
AB - PUF proteins, a family of RNA-binding proteins, interact with the 3′ untranslated regions (UTRs) of specific mRNAs to control their translation and stability. PUF protein action is commonly correlated with removal of the poly(A) tail of target mRNAs. Here, we focus on how PUF proteins enhance deadenylation and mRNA decay. We show that a yeast PUF protein physically binds Pop2p, which is a component of the Ccr4p-Pop2p-Not deadenylase complex, and that Pop2p is required for PUF repression activity. By binding Pop2p, the PUF protein simultaneously recruits the Ccr4p deadenylase and two other enzymes involved in mRNA regulation, Dcp1p and Dhh1p. We reconstitute regulated deadenylation in vitro and demonstrate that the PUF-Pop2p interaction is conserved in yeast, worms and humans. We suggest that the PUF-Pop2p interaction underlies regulated deadenylation, mRNA decay and repression by PUF proteins.
UR - http://www.scopus.com/inward/record.url?scp=33744946810&partnerID=8YFLogxK
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U2 - 10.1038/nsmb1100
DO - 10.1038/nsmb1100
M3 - Article
VL - 13
SP - 533
EP - 539
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 6
ER -