Literature DB >> 16789907

pEg6, a spire family member, is a maternal gene encoding a vegetally localized mRNA in Xenopus embryos.

Catherine Le Goff1, Véronique Laurent, Kristell Le Bon, Gaëlle Tanguy, Anne Couturier, Xavier Le Goff, René Le Guellec.   

Abstract

BACKGROUND INFORMATION: In Xenopus, during oocyte maturation and the segmentation period, cell cycle progression is independent of new transcription, but requires de novo translation. This suggests that the completion of oocyte maturation and then the rapid cell division period is controlled exclusively at a post-transcriptional level by specific gene products. To isolate these maternal genes, a differential screening of a Xenopus egg cDNA library was performed. Several cDNAs were isolated which correspond to mRNA polyadenylated in eggs and deadenylated in embryos, and these constitute the founders members of the Eg family of mRNAs.
RESULTS: We report here the characterization of Eg6 mRNA as a novel maternal gene expressed in Xenopus egg until gastrula stage. The Eg6 transcript is initially concentrated in the vegetal cytoplasm of the egg, and later the distribution of the transcript marks the posterior vegetal end of developing embryos. pEg6 is a multidomain protein with a kinase non-catalytic C-lobe domain of unknown function, a cluster of four WH2 (Wiskott-Aldrich syndrome protein homology 2) domains and a modified FYVE zinc-finger motif. The amino acid sequence of pEg6 is related to PEM-5 (posterior end mark-5), from an ascidian maternal mRNA, and spire, a Drosophila protein required to establish dorsal-ventral and anterior-posterior axes of polarity and recently described as an actin nucleation factor. In Xenopus and Schizosaccharomyces pombe cells pEg6 expression induces filamentous actin clusters and is associated with vesicular structure.
CONCLUSION: These data suggest that pEg6 acts as a vegetally localized factor contributing to the actin nucleation process during Xenopus early development.

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Year:  2006        PMID: 16789907     DOI: 10.1042/BC20050095

Source DB:  PubMed          Journal:  Biol Cell        ISSN: 0248-4900            Impact factor:   4.458


  4 in total

1.  Multiple forms of Spire-actin complexes and their functional consequences.

Authors:  Christine K Chen; Michael R Sawaya; Martin L Phillips; Emil Reisler; Margot E Quinlan
Journal:  J Biol Chem       Date:  2012-02-08       Impact factor: 5.157

2.  Structure and function of the interacting domains of Spire and Fmn-family formins.

Authors:  Christina L Vizcarra; Barry Kreutz; Avital A Rodal; Angela V Toms; Jun Lu; Wei Zheng; Margot E Quinlan; Michael J Eck
Journal:  Proc Natl Acad Sci U S A       Date:  2011-07-05       Impact factor: 11.205

3.  Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins.

Authors:  Markos Pechlivanis; Annette Samol; Eugen Kerkhoff
Journal:  J Biol Chem       Date:  2009-07-15       Impact factor: 5.157

4.  Regulatory interactions between two actin nucleators, Spire and Cappuccino.

Authors:  Margot E Quinlan; Susanne Hilgert; Anaid Bedrossian; R Dyche Mullins; Eugen Kerkhoff
Journal:  J Cell Biol       Date:  2007-10-08       Impact factor: 10.539

  4 in total

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