Poly(A)^+-Binding Proteins from Seedlings of Winter Wheat
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概要
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In the preceding paper, we described the fractionation of oligo(dT)-binding proteins(Oligo(dT)BP)from seedlings of winter wheat by chromatography on oligo(dT)-cellulose according to the procedure of Jeffery(1977); one fraction(designated as fraction D)was eluted in buffer D(10mM Tris-HCl, pH 7.4), and the other(the formamide fraction)was eluted in the same buffer supplemented with 500 g L^<-1> formamide. Oligo(dT)BPs from the wheat seedlings in each fraction showed differences in the polypeptide composition. Eucaryotic mRNAs in their functional forms consisted of ribonucleoprotein complexes(Jeffery 1977; Van Venrooij et al.1977; Baer and Kornberg 1980; Vincent et al.1981). Major proteins in these complexes consist of poly(A)^+-binding proteins(Poly(A)BPs), which bind to the 3′ poly(A) "tail" (Bernstein and Ross 1989). Poly(A)BPs have been identified in many species(Bernstein and Ross 1989; Drawbridge et al.1990). In Saccharomyces cerevisiae, Poly(A)BPs are essential for cell viability and are considered to influence a wide variety of cellular processes that are involved in the turnover of mRNA, recruitment of ribosomal subunits, and translation(Sachs et al.1987; Sachs and Davis 1989; Bernstein et al.1989; Munroe and Jacobson 1990). Since the discovery of the poly(A)^+-binding proteins(PABPs)associated with rabbit globin mRNA(Blobel 1973), most of the information about PABPs has been generated from studies on eucaryotes, such as Drosophila melanogaster(Drawbridge et al.1990), human(Grange et al.1987), Strongylocentrotus purpuratus(Drawbridge et al.1990), Xenopus laevis(Zelus et al.1989), and yeast(Sachs et al.1987). In spite of their importance in the regulation of translation, little is known about the PABPs and poly(A)BPs of higher plants. PABPs fractionated from embryonic axes of dry pea seeds(Pisum sativum)contained 60-kDa proteins(Sieliwanowicz 1987) that stimulated the translational activity in a cell-free system. Moreover, Yang and Hunt(1991)purified a 70-kDa protein from seedlings of the same plant with a high poly(A)-binding activity. This report describes the separation of poly(A) "tails" from cytoplasmic Oligo(dT)BPs (it seems more appropriate to use the term "oligo(dT)-binding proteins" than poly(A)^+-RNA-binding proteins in the present paper), and an analysis of the polypeptide composition of Poly(A)BPs.
- 社団法人日本土壌肥料学会の論文
著者
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SAGISAKA Shonosuke
The Institute of Low Temperature Science, Hokkaido University
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Sagisaka Shonosuke
The Institute Of Lou Temperature Science Hokkaido University
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Okuda Tohru
The Institute Of Low Temperature Science Hokkaido University
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Okuda Tohru
The Institute Of Enology And Viticulture Yamanashi University
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Yamanaka Akira
The Institute Of Low Temperature Science Hokkaido University
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Sagisaka S
The Institute Of Low Temperature Science Hokkaido University
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Matsuda Yusuke
The Institute of Low Temperature Science, Hokkaido University
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Matsuda Y
Iwate Univ. Morioka Jpn
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