Xp54, the Xenopus Homologue of Human RNA Helicase p54, is an Integral Component of Stored mRNP Particles in Oocytes

Ladomery, Michael; Wade, Eleanor; Sommerville, John

doi:10.1093/nar/25.5.965

Cited by 138 publications

(131 citation statements)

References 37 publications

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“…Minshall et al already reported the interaction of Xp54 with eIF4E in Xenopus oocytes (27). In the current study, we also demonstrated the interaction of rck/p54 with eIF4E.…”

Section: Discussionsupporting

confidence: 85%

“…rck/p54 belongs to the RNA helicase SF2/DDX6 subfamily, which is highly conserved from trypanonosomes to humans (15). This subfamily includes Xenopus Xp54 (27), Drosophilla Me31B (28), C. elegans Chh-1 (29) and Saccharomyces cerevisisae Dhh-1 (24). Members of the DEAD-box superfamily are involved in a variety of cellular processes, including splicing, ribosome biosynthesis, RNA transport, translation initiation and RNA decay.…”

Section: Discussionmentioning

confidence: 99%

“…Xenopus Xp54, an integral component of stored mRNP in oocytes, is present at constant levels throughout oogenesis (27). This RNA helicase was shown to possess ATP-dependent duplex unwinding activity, to be a shuttling protein implicated in the nuclear assembly of stored mRNP particles and, further, to repress translation 3-to 5-fold; however, mutations in its DEAD and HRIGR helicase motifs activated translation to a 3-to 4-fold greater extent relative to the control (30).…”

Section: Discussionmentioning

confidence: 99%

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Human DEAD-box/RNA unwindase rck/p54 contributes to maintenance of cell growth by affecting cell cycle in cultured cells

Akao¹,

Matsumoto²,

Ohguchi³

et al. 2006

Int J Oncol

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Abstract. Understanding the control of gene expression in cancer cells requires defining the molecular and cellular basis of RNA metabolism compared with that in steady-state normal cells. Previously, we reported evidence that human RNA structure-modifying unwindase rck/p54, a member of the DEAD-box family, was highly expressed in most of the malignant cell lines tested and that this expression was linked to malignant transformation. Here, we show that rck/p54 positively affects cell growth, probably by modulating the gene expression at the translational level in cultured cells. In cell growth and differentiation induced by external stimuli, the level of rck/p54 expression was up-regulated during cell proliferation and down-regulated during differentiation. The down-regulation of rck/p54 in HeLa cells by RNAi induced cell growth inhibition through cell cycle arrest at S phase. Immunoprecipitation using anti-rck/p54 antibody in HeLa cells demonstrated the co-precipitation of rck/p54 with eIF4E, which is well-known to bind to the 5'cap-structure, resulting in initiation of translation. These data suggest that rck/p54 contributes to cell growth possibly by modulating translationinitiation control of the genes involved in the cell proliferation, which is a newly defined mechanism leading to carcinogenesis.

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“…Minshall et al already reported the interaction of Xp54 with eIF4E in Xenopus oocytes (27). In the current study, we also demonstrated the interaction of rck/p54 with eIF4E.…”

Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Human DEAD-box/RNA unwindase rck/p54 contributes to maintenance of cell growth by affecting cell cycle in cultured cells

Akao¹,

Matsumoto²,

Ohguchi³

et al. 2006

Int J Oncol

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“…ZDS2 and ZDS1 are required for G 2 /M progression and SWE1 function and can suppress mutations in numerous genes, mostly cell cycle regulators (Bi and Pringle, 1996;Ma et al, 1996;Schwer and Shuman, 1996;Yu et al, 1996;Mizunuma et al, 1998;Roy and Runge, 2000, and references within). DHH1 is a non-essential DEAD-box helicase that has been implicated in SWE1 function (Strahl-Bolsinger and Tanner, 1993;Warbick and Glover, 1994;Moriya and Isono, 1999), translation (Ladomery et al, 1997), transcription (Hata et al, 1998) and cell cycle arrest under stressful conditions (Maekawa et al, 1994;Bergkessel and Reese, unpublished). RPN11 encodes a regulatory subunit of the 26S proteasome that is required for G 2 /M progression (Glickman et al, 1998;Rinaldi et al, 1998) and for the activation of the transcription factor Gcn4p by UV-induced stress (Stitzel et al, 2001).…”

Section: Isolation Of High Copy Suppressors Of the Taf68-9 Mutantmentioning

confidence: 99%

Genetic analysis of TAF68/61 reveals links to cell cycle regulators

Reese

Green

2001

Yeast

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In yeast, inactivation of certain TBP-associated factors (TAF II s) results in arrest at specific stages of the cell cycle. In some cases, cell cycle arrest is not observed because overlapping defects in other cellular processes precludes the manifestation of an arrest phenotype. In the latter situation, genetic analysis has the potential to reveal the involvement of TAF II s in cell cycle regulation. In this report, a temperature-sensitive mutant of TAF68/61 was used to screen for high-copy dosage suppressors of its growth defect. Ten genes were isolated: TAF suppressor genes, TSGs 1-10. Remarkably, most TSGs have either a genetic or a direct link to control of the G 2 /M transition. Moreover, eight of the 10 TSGs can suppress a CDC28 mutant specifically defective for mitosis (cdc28-1N) but not an allele defective for passage through start. The identification of these genes as suppressors of cdc28-1N has identified four unreported suppressors of this allele. Moreover, synthetic lethality is observed between taf68-9 and cdc28-1N. The isolation of multiple genes involved in the control of a specific phase of the cell cycle argue that the arrest phenotypes of certain TAF II mutants reflect their role in specifically regulating cell cycle functions.

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“…The addition of a sufficient excess of Y-box proteins into in vitro translation systems leads to a translational repression of reporter mRNAs (20 -22). Later studies identified other components of mRNPs, including a DEAD-box ATPase Xp54 and embryonic poly(A)-binding proteins, ePAB and ePABP2 (23)(24)(25)(26)(27). Xp54 and its human homologue RCK repress translation in vitro and/or in oocytes (28,29).…”

mentioning

confidence: 99%

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

Tanaka

Ogawa

Takagi

et al. 2006

Journal of Biological Chemistry

106

128

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mRNAs in eukaryotic cells are presumed to always associate with a set of proteins to form mRNPs. In Xenopus oocytes, a large pool of maternal mRNAs is masked from the translational apparatus as storage mRNPs. Here we identified Xenopus RAP55 (xRAP55) as a component of RNPs that associate with FRGY2, the principal component of maternal mRNPs. RAP55 is a member of the Scd6 or Lsm14 family. RAP55 localized to cytoplasmic foci in Xenopus oocytes and the processing bodies (P-bodies) in cultured human cells: in the latter cells, RAP55 is an essential constituent of the P-bodies. We isolated xRAP55-containing complexes from Xenopus oocytes and identified xRAP55-associated proteins, including a DEAD-box protein, Xp54, and a protein arginine methyltransferase, PRMT1. Recombinant xRAP55 repressed translation, together with Xp54, in an in vitro translation system. In addition, xRAP55 repressed translation in oocytes when tethered with a reporter mRNA. Domain analyses revealed that the N-terminal region of RAP55, including the Lsm domain, is important for the localization to P-bodies and translational repression. Taken together, our results suggest that xRAP55 is involved in translational repression of mRNA as a component of storage mRNPs.

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Xp54, the Xenopus Homologue of Human RNA Helicase p54, is an Integral Component of Stored mRNP Particles in Oocytes

Cited by 138 publications

References 37 publications

Human DEAD-box/RNA unwindase rck/p54 contributes to maintenance of cell growth by affecting cell cycle in cultured cells

Human DEAD-box/RNA unwindase rck/p54 contributes to maintenance of cell growth by affecting cell cycle in cultured cells

Genetic analysis of TAF68/61 reveals links to cell cycle regulators

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

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