ArticlePlant physiology1992
Purification and Characterization of a 70-Kilodalton Polyadenylate-Binding Protein from Pea (Pisum sativum).
Article in Plant physiology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro.Plant molecular biology · 1996Article
- Identification of a 67 kDa protein that binds specifically to the pre-rRNA primary processing site in a higher plant.Nucleic acids research · 1995Article
- Binding of a 50-kD Protein to a U-Rich Sequence in an mRNA Encoding a Proline-Rich Protein That Is Destabilized by Fungal Elicitor.The Plant cell · 1994Article
- Control of mRNA Stability in Higher Plants.Plant physiology · 1993Article
- Differential organ-specific expression of three poly(A)-binding-protein genes from Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A polyadenylate-binding protein (PABP) was purified from cell-free extracts prepared from pea seedlings (Pisum sativum) by ammonium sulfate precipitation and Affi-Gel Blue and polyadenylate-Sepharose 4B affinity chromatography. The final preparation from polyadenylate-Sepharose 4B columns contained a single 70-kilodalton polypeptide with high polyadenylate-binding activity. The purified protein was active over a broad range of ionic strengths and showed temperature and pH optima of 37 degrees C and pH 6.5, respectively. Specificity studies indicated that the pea PABP was most active with polyadenylic acids, showed some activity with polyguanylic acid, and did not bind to polycytidylic acid. Moreover, longer polyadenylate molecules were bound more effectively than shorter ones. Because these properties are similar to PABPs isolated from other sources, we conclude that we have identified, purified, and characterized a plant PABP analogous to those described in yeast and animal systems.
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Registered trials
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