Two Yeast PUF Proteins Negatively Regulate a Single mRNA

Hook, Brad; Goldstrohm, Aaron C.; Seay, Daniel J.; Wickens, Marvin

doi:10.1074/jbc.m611253200

Cited by 80 publications

(138 citation statements)

References 37 publications

(51 reference statements)

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“…Repression by Puf4p is dependent on deadenylation, whereas repression by Puf5p is not (3)(4)(5). Thus, the information embedded in the binding element specifies which form of repression occurs.…”

Section: Discussionmentioning

confidence: 99%

“…These proteins bind elements in 3′ untranslated regions (3′UTRs), termed PUF binding elements (PBEs) (1,2). PUFs commonly repress translation or enhance mRNA decay (3)(4)(5)(6)(7)(8) but also can activate and localize mRNAs (7,(9)(10)(11)(12)(13)(14). The six PUF proteins of Saccharomyces cerevisiae control distinct sets of RNAs that comprise distinct functional groups and bind ∼850 mRNAs, or 10-15% of the mRNA species in that organism (15,16).…”

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confidence: 99%

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Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site

Valley¹,

Porter

Qiu

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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mRNA control hinges on the specificity and affinity of proteins for their RNA binding sites. Regulatory proteins must bind their own sites and reject even closely related noncognate sites. In the PUF [Pumilio and fem-3 binding factor (FBF)] family of RNA binding proteins, individual proteins discriminate differences in the length and sequence of binding sites, allowing each PUF to bind a distinct battery of mRNAs. Here, we show that despite these differences, the pattern of RNA interactions is conserved among PUF proteins: the two ends of the PUF protein make critical contacts with the two ends of the RNA sites. Despite this conserved "two-handed" pattern of recognition, the RNA sequence is flexible. Among the binding sites of yeast Puf4p, RNA sequence dictates the pattern in which RNA bases are flipped away from the binding surface of the protein. Small differences in RNA sequence allow new modes of control, recruiting Puf5p in addition to Puf4p to a single site. This embedded information adds a new layer of biological meaning to the connections between RNA targets and PUF proteins.mRNA turnover | RNA regulation | translation | 3′UTR elements

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Patterns and plasticity in RNA-protein interactions enable recruitment of multiple proteins through a single site

Valley¹,

Porter

Qiu

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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“…Together our results suggest that FBF repression relies, at least in part, on the deadenylation of target mRNAs. In yeast, PUF-mediated repression is similarly dependent on Pop2p to promote deadenylation, degradation, and translational repression of target mRNA (Goldstrohm et al 2006Hook et al 2007). Furthermore, both human and Drosophila PUF proteins bind directly to the relevant Pop2p/Caf1 homolog (Goldstrohm et al 2006;Kadyrova et al 2007).…”

Section: Discussionmentioning

confidence: 99%

FBF and Its Dual Control of gld-1 Expression in the Caenorhabditis elegans Germline

Suh

Crittenden

Goldstrohm³

et al. 2009

Genetics

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FBF, a PUF RNA-binding protein, is a key regulator of the mitosis/meiosis decision in the Caenorhabditis elegans germline. Genetically, FBF has a dual role in this decision: it maintains germ cells in mitosis, but it also facilitates entry into meiosis. In this article, we explore the molecular basis of that dual role. Previous work showed that FBF downregulates gld-1 expression to promote mitosis and that the GLD-2 poly(A) polymerase upregulates gld-1 expression to reinforce the decision to enter meiosis. Here we ask whether FBF can act as both a negative regulator and a positive regulator of gld-1 expression and also investigate its molecular mechanisms of control. We first show that FBF co-immunoprecipitates with gld-1 mRNA, a result that complements previous evidence that FBF directly controls gld-1 mRNA. Then we show that FBF represses gld-1 expression, that FBF physically interacts with the CCF-1/Pop2p deadenylase and can stimulate deadenylation in vitro, and that CCF-1 is partially responsible for maintaining low GLD-1 in the mitotic region. Finally, we show that FBF can elevate gld-1 expression, that FBF physically interacts with the GLD-2 poly(A) polymerase, and that FBF can enhance GLD-2 poly(A) polymerase activity in vitro. We propose that FBF can affect polyadenylation either negatively by its CCF-1 interaction or positively by its GLD-2 interaction.

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“…Recent studies on Puf protein-mediated post-transcriptional processing uncovered the role of Puf proteins as cytoplasmic deadenylation cofactors. [4][5][6][7] De-adenylation of mRNA in eukaryotic cytoplasm accompanies translational repression and/or decay of mRNAs, and thus eventually regulates growth and development. In budding yeast, Puf4p and Mpt5 (Puf5p) are components of the Pop2p-Ccr4-Not de-adenylase complex, which removes the poly(A) tail of target mRNA and also recruits DExD/H-box helicase 1 (Dhh1p) and decapping enzyme 1 (Dcp1) for translational repression.…”

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confidence: 99%