Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells

Nakanishi, Teruyuki; Kumagai, Satoshi; Kimura, Masanori; Watanabe, Hiromi; Sakurai, Takayuki; Kimura, Minoru; Kashiwabara, Shin‐ichi; Baba, Tadashi

doi:10.1016/j.bbrc.2007.09.096

Cited by 41 publications

(41 citation statements)

References 22 publications

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“…Silencing the other candidate transferase genes had no effect on the composition of the 39 termini of 7SL RNA, although it was reported previously that SRP-RNA-AE is responsible for 39 adenylation of 7SL RNA in vitro (Perumal et al 2001). To confirm the effects of reduced GLD-2 expression in mouse, we analyzed 7SL RNA isolated from the livers of mGLD-2 knockout mice (Nakanishi et al 2007). When compared with the result from heterozygous mGLD-2 +/À mice, the proportions of the two 39-A fragments (UCUCUa and UCUCUua) were substantially lower, and the proportion of UCUCUu was 7À (m/z 1073.9) was selected as a precursor mass for CID.…”

Section: Resultsmentioning

confidence: 96%

“…In addition, mouse GLD-2 has been suggested to control the translation of specific mRNAs during oogenesis (Nakanishi et al 2006). However, disruption of mGLD-2 had no effect on full-term development and oogenesis, implying that another cytoplasmic poly(A) polymerase is redundantly required for oogenesis in mouse (Nakanishi et al 2007). Thus, the functional roles played by mammalian GLD-2 were unclear.…”

Section: Resultsmentioning

confidence: 99%

“…Homozygous (À/À) and heterozygous (+/À) mice lacking mGLD-2 were prepared as described previously (Nakanishi et al 2007). Total RNAs were isolated from homogenized mouse livers from both mGLD-2 +/À and mGLD-2 À/À mice using Trizol reagent (Invitrogen).…”

Section: Mgld-2 Knockout Mousementioning

confidence: 99%

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Selective stabilization of mammalian microRNAs by 3′ adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2

Katoh¹,

Sakaguchi²,

Miyauchi³

et al. 2009

Genes Dev.

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398

395

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The steady-state levels of microRNAs (miRNAs) and their activities are regulated by the post-transcriptional processes. It is known that 39 ends of several miRNAs undergo post-dicing adenylation or uridylation. We isolated the liver-specific miR-122 from human hepatocytes and mouse livers. Direct analysis by mass spectrometry revealed that one variant of miR-122 has a 39-terminal adenosine that is introduced after processing by Dicer. We identified GLD-2, which is a regulatory cytoplasmic poly(A) polymerase, as responsible for the 39-terminal adenylation of miR-122 after unwinding of the miR-122/ miR-122* duplex. In livers from GLD-2-null mice, the steady-state level of the mature form of miR-122 was specifically lower than in heterozygous mice, whereas no reduction of pre-miR-122 was observed, demonstrating that 39-terminal adenylation by GLD-2 is required for the selective stabilization of miR-122 in the liver.Supplemental material is available at http://www.genesdev.org.

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Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Selective stabilization of mammalian microRNAs by 3′ adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2

Katoh¹,

Sakaguchi²,

Miyauchi³

et al. 2009

Genes Dev.

Self Cite

398

395

View full text Add to dashboard Cite

show abstract

“…), the functional correlates of this interaction have yet to be formally tested. In this regard, it is worth noting that there is no phenotype associated with the homozygous deletion of GLD2 in the mouse (Nakanishi et al 2007), implying that functional redundancy exists in mammalian cells. It will thus be necessary to develop new approaches and experimental models to overcome these difficulties in order to explore possible role(s) for aCP2 in mammalian somatic cytoplasmic polyadenylation and resulting cytoplasmic controls.…”

Section: Xacp2 Is a Novel Mediator Of The Cytoplasmic Polyadenylationmentioning

confidence: 99%

The poly(rC)-binding protein αCP2 is a noncanonical factor in X. laevis cytoplasmic polyadenylation

Vishnu

Sumaroka²,

Klein³

et al. 2011

RNA

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Post-transcriptional control of mRNA stability and translation is central to multiple developmental pathways. This control can be linked to cytoplasmic polyadenylation in certain settings. In maturing Xenopus oocytes, specific mRNAs are targeted for polyadenylation via recruitment of the Cytoplasmic Polyadenylation Element (CPE) binding protein (CPEB) to CPE(s) within the 39 UTR. Cytoplasmic polyadenylation is also critical to early embryonic events, although corresponding determinants are less defined. Here, we demonstrate that the Xenopus ortholog of the poly(rC) binding protein aCP2 can recruit cytoplasmic poly(A) polymerase activity to mRNAs in Xenopus post-fertilization embryos, and that this recruitment relies on cis sequences recognized by aCP2. We find that the ha-globin 39 UTR, a validated mammalian aCP2 target, constitutes an effective target for cytoplasmic polyadenylation in Xenopus embryos, but not during Xenopus oocyte maturation. We further demonstrate that the cytoplasmic polyadenylation activity is dependent on the action of the C-rich aCP-binding site in conjunction with the adjacent AAUAAA. Consistent with its ability to target mRNA for poly(A) addition, we find that XaCP2 associates with core components of the Xenopus cytoplasmic polyadenylation complex, including the cytoplasmic poly(A) polymerase XGLD2. Furthermore, we observe that the C-rich aCP-binding site can robustly enhance the activity of a weak canonical oocyte maturation CPE in early embryos, possibly via a direct interaction between XaCP2 and CPEB1. These studies establish XaCP2 as a novel cytoplasmic polyadenylation trans factor, indicate that C-rich sequences can function as noncanonical cytoplasmic polyadenylation elements, and expand our understanding of the complexities underlying cytoplasmic polyadenylation in specific developmental settings.

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“…The eggs were placed in FHM medium [35], treated briefly with 0.01% bovine hyaluronidase (Sigma-Aldrich, St. Louis, MO, USA), microinjected with RNAs (approximately 10 pl) using a Piezo-driven micromanipulator (PrimeTech, Ibaraki, Japan) and then incubated in drops of kSOM medium [35] covered with mineral oil (Sigma-Aldrich) at 37 C under 5% CO2 in air. All animal experiments were carried out according to the Guide for the Care and Use of Laboratory Animals at the University of Tsukuba.…”

Section: Egg Collection and Microinjectionmentioning

confidence: 99%

Birth of Normal Offspring from Mouse Eggs Activated by a Phospholipase C.ZETA. Protein Lacking Three EF-hand Domains

Nakanishi

Ishibashi

Kubota

et al. 2008

Journal of Reproduction and Development

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Abstract. Sperm-specific phospholipase C, PLCζ, is a candidate for the Ca 2+ oscillation-inducing factor that is introduced into the ooplasm upon sperm-egg fusion. In addition to the 647-residue full-length PLCζ, s-PLCζ lacking the N-terminal 110 amino acids is known to be present in the mouse testis. In this study, we attempted to obtain fullterm offspring from s-PLCζ-activated eggs by round spermatid injection. Metaphase II-arrested eggs injected with a high RNA concentration of s-PLCζ RNA normally developed to blastocysts. When the round spermatid nucleus was injected into telophase II-stage eggs previously activated by s-PLCζ RNA, three live offspring were successfully obtained by transfer of the developed 4-cell embryos to pseudopregnant mice. These three offspring all grew to be normal adults and reproduced healthy second-generation mice.

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Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells

Abstract: 14The elongation of poly(A) tails in cytoplasm is essential for oogenesis and early

Cited by 41 publications

References 22 publications

Selective stabilization of mammalian microRNAs by 3′ adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2

Selective stabilization of mammalian microRNAs by 3′ adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2

The poly(rC)-binding protein αCP2 is a noncanonical factor in X. laevis cytoplasmic polyadenylation

Birth of Normal Offspring from Mouse Eggs Activated by a Phospholipase C.ZETA. Protein Lacking Three EF-hand Domains

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