Analysis of mRNA associated factors during bovine oocyte maturation and early embryonic development
| Autor: | Monika Bhojwani, Tatjana Smiljakovic, Corinna Siemer, Wolfgang Tomek, Wilhelm Kanitz, Claus Leiding, Michal Kubelka |
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| Rok vydání: | 2009 |
| Předmět: |
Male
RNA Caps Repressor Embryonic Development Fertilization in Vitro Biology chemistry.chemical_compound Cyclin-dependent kinase Pregnancy Genetics Animals RNA Messenger Regulation of gene expression Kinase EIF4G EIF4E Gene Expression Regulation Developmental RNA-Binding Proteins Cell Biology Molecular biology chemistry eIF4A biology.protein Oocytes Phosphorylation Cattle Female Protein Kinases Developmental Biology |
| Zdroj: | Molecular reproduction and development. 76(12) |
| ISSN: | 1098-2795 |
| Popis: | Regulation of gene expression at the translational level is particularly essential during developmental periods, when transcription is impaired. According to the closed-loop model of translational initiation, we have analyzed components of the 5 -mRNA cap-binding complex eIF4F (eIF4E, eIF4G, eIF4A), the eIF4E repressor 4E-BP1, and 3 -mRNA poly-(A) tail-associated proteins (PABP1 and 3, PAIP1 and 2, CPEB1, Maskin) during in vitro maturation of bovine oocytes and early embryonic development up to the 16-cell stage. Furthermore, we have elucidated the activity of distinct kinases which are potentially involved in their phosphorylation. Major phosphorylation of specific target sequences of PKA, PKB, PKC, CDKs, ATM/ATR, and MAPK were observed in M II stage oocytes. Furthermore, main changes in the abundance and/or phosphorylation of distinct mRNA-binding factors occur at the transition from M II stage oocytes to 2-cell embryos. In conclusion, the results indicate that, at the transition from oocyte to embryonic development, translational initiation is regulated by striking differences in the abundance and/or phosphorylation of 5 -end and 3 -end mRNA associated factors, mainly the poly-(A) bindings proteins PABP1 and 3, their repressor PAIP2 and a Maskin-like protein with distinct eIF4E-binding properties which prevents eIF4E/cap binding and eIF4F formation in vitro. Nevertheless, from the M II stage to 16-cell embryos a substantial amount of eIF4E and, to a lesser extent, of eIF4G was precipitated by (7)m-GTP-Separose indicating eIF4F complex formation. Therefore, it is likely that in general the reduction in PABP1 and 3 abundance represses overall translation during early embryonic development. |
| Databáze: | OpenAIRE |
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