Conservation of the deadenylase activity of proteins of the Caf1 family in human

Bianchin, Claire; Mauxion, Fabienne; Sentis, Stéphanie; Séraphin, Bertrand; Corbo, Laura

doi:10.1261/rna.7135305

Cited by 86 publications

(87 citation statements)

References 34 publications

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“…CCF-1 possesses a DEDD-type, magnesium-dependent exoribonuclease domain and shares significant sequence identity with other Pop2p orthologs ( Figure 3, A and B). Mammalian Pop2 is an enzymatically active deadenylase (Thore et al 2003;Viswanathan et al 2004;Bianchin et al 2005). Since CCF-1 contains all active site residues ( Figure 3A), it too is likely an active deadenylase.…”

Section: Fbf-1 Co-immunoprecipitates With Gld-1 Mrnamentioning

confidence: 99%

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

Suh

Crittenden

Goldstrohm³

et al. 2009

Genetics

125

168

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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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Section: Fbf-1 Co-immunoprecipitates With Gld-1 Mrnamentioning

confidence: 99%

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

Suh

Crittenden

Goldstrohm³

et al. 2009

Genetics

125

168

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“…While much less is known about the RNA turnover processes in S. pombe, the strong conservation of the caf1 gene and the Ccr4-Not complex in eukaryotes from yeast to humans led us to suggest that Pop2p maintains a similar function in S. pombe as has been observed in other eukaryotes (Albert et al 2000;Bianchin et al 2005). Most importantly, the S. pombe ortholog has a fully conserved DEDDh active site, and combined structural and functional data subsequently showed that the protein is a functional 39-59 exonuclease specific to RNA with a tuneable preference for poly-A sequences (Jonstrup et al 2007).…”

Section: Introductionmentioning

confidence: 96%

The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn²⁺ and Mn²⁺ in the active site

Andersen

Jonstrup²,

Van³

et al. 2009

RNA

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In eukaryotic organisms, initiation of mRNA turnover is controlled by progressive shortening of the poly-A tail, a process involving the mega-Dalton Ccr4-Not complex and its two associated 39-59 exonucleases, Ccr4p and Pop2p (Caf1p). RNA degradation by the 39-59 DEDDh exonuclease, Pop2p, is governed by the classical two metal ion mechanism traditionally assumed to be dependent on Mg 2+ ions bound in the active site. Here, we show biochemically and structurally that fission yeast (Schizosaccharomyces pombe) Pop2p prefers Mn 2+ and Zn 2+ over Mg 2+ at the concentrations of the ions found inside cells and that the identity of the ions in the active site affects the activity of the enzyme. Ion replacement experiments further suggest that mRNA deadenylation could be subtly regulated by local Zn 2+ levels in the cell. Finally, we use site-directed mutagenesis to propose a mechanistic model for the basis of the preference for poly-A sequences exhibited by the Pop2p-type deadenylases as well as their distributive enzymatic behavior.

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“…The two CAF1 proteins seem to be integrated into the CCR4-NOT complex in a mutually exclusive manner, and the same is true for the two CCR4 proteins (Lau et al 2009). All four proteins are active as deadenylases in vitro (Viswanathan et al 2003Bianchin et al 2005;Morita et al 2007). They play overlapping roles in mRNA deadenylation, and their catalytic activities are essential for their in vivo functions, as shown by dominant-negative effects of mutant variants (Yamashita et al 2005;Morita et al 2007;Mauxion et al 2008;Schwede et al 2008;Zheng et al 2008;Aslam et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation

Temme¹,

Zhang²,

Kremmer³

et al. 2010

RNA

147

198

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The CCR4-NOT complex is the main enzyme catalyzing the deadenylation of mRNA. We have investigated the composition of this complex in Drosophila melanogaster by immunoprecipitation with a monoclonal antibody directed against NOT1. The CCR4, CAF1 (=POP2), NOT1, NOT2, NOT3, and CAF40 subunits were associated in a stable complex, but NOT4 was not. Factors known to be involved in mRNA regulation were prominent among the other proteins coprecipitated with the CCR4-NOT complex, as analyzed by mass spectrometry. The complex was localized mostly in the cytoplasm but did not appear to be a major component of P bodies. Of the known CCR4 paralogs, Nocturnin was found associated with the subunits of the CCR4-NOT complex, whereas Angel and 3635 were not. RNAi experiments in Schneider cells showed that CAF1, NOT1, NOT2, and NOT3 are required for bulk poly(A) shortening and hsp70 mRNA deadenylation, but knock-down of CCR4, CAF40, and NOT4 did not affect these processes. Overexpression of catalytically dead CAF1 had a dominant-negative effect on mRNA decay. In contrast, overexpression of inactive CCR4 had no effect. We conclude that CAF1 is the major catalytically important subunit of the CCR4-NOT complex in Drosophila Schneider cells. Nocturnin may also be involved in mRNA deadenylation, whereas there is no evidence for a similar role of Angel and 3635.

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Conservation of the deadenylase activity of proteins of the Caf1 family in human

Cited by 86 publications

References 34 publications

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

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

The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn²⁺ and Mn²⁺ in the active site

Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation

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Conservation of the deadenylase activity of proteins of the Caf1 family in human

Cited by 86 publications

References 34 publications

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

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

The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site

Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation

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The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn²⁺ and Mn²⁺ in the active site