ArticleThe Biochemical journal1992
Purification and characterization of recombinant Xenopus poly(A)(+)-binding protein expressed in a baculovirus system.
Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Translational activation of maternally derived mRNAs in oocytes and early embryos and the role of embryonic poly(A) binding protein (EPAB).Biology of reproduction · 2019Review
- Epab and Pabpc1 are differentially expressed during male germ cell development.Reproductive sciences (Thousand Oaks, Calif.) · 2012Article
- Identification and characterization of human embryonic poly(A) binding protein (EPAB).Molecular human reproduction · 2008Article
- Dendritic BC1 RNA in translational control mechanisms.The Journal of cell biology · 2005Article
- An embryonic poly(A)-binding protein (ePAB) is expressed in mouse oocytes and early preimplantation embryos.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The mechanism and regulation of deadenylation: identification and characterization of Xenopus PARN.RNA (New York, N.Y.) · 2001Article
- Levels of free PABP are limited by newly polyadenylated mRNA in early Spisula embryogenesis.Nucleic acids research · 2000Article
- The role of 5'-leader length, secondary structure and PABP concentration on cap and poly(A) tail function during translation in Xenopus oocytes.Nucleic acids research · 2000Article
- Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes.The EMBO journal · 1996Article
- Human immunodeficiency virus type 1 Rev is required in vivo for binding of poly(A)-binding protein to Rev-dependent RNAs.Journal of virology · 1994Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The poly(A)(+)-binding protein (PABP) is a highly conserved protein that binds to the poly(A)+ tail of mRNAs. PABP has been shown to regulate message stability and translational efficiency, yet the mechanisms remain unknown. To facilitate further dissection of the functions of this protein, we have expressed and purified Xenopus PABP using a baculovirus expression system. At 48 h after infection of insect Spodoptera frugiperda (Sf9) cells with recombinant virus, approx. 3% of cell protein was PABP. Purification of PABP was achieved by affinity chromatography on poly(A)(+)-Sepharose. The purified protein was indistinguishable from Xenopus PABP with respect to its immunoreactivity and electrophoretic mobility. Furthermore, the recombinant PABP was expressed and purified as a functional protein as indicated by its ability to bind to poly(A)(+)-Sepharose and its ability to enhance the translation of adenylated messages in vitro. By comparing protein extracts from various developmental stages of Xenopus embryos with known amounts of purified PABP, we determined the amount of PABP per embryo. This analysis suggested that there is less than one PABP molecule available per PABP-binding site at early stages of development, and only a slight excess of PABP at later stages.
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