Abstract
Western blots of soluble protein from wheat, rice, and corn showed that ADPglucose pyrophosphorylase subunits have a size of 50 kilodaltons from endosperm tissue and 43 and 46 kilodaltons from leaf. Antisera to ADPglucose pyrophosphorylase precipitated in vitro translation products of 73 and 76 kilodaltons when leaf poly(A)+ RNA was used, whereas endosperm mRNA directed the synthesis of 50 and 56 kilodalton polypeptides. To further study the nature of these mRNA species, an ADPglucose pyrophosphorylase cDNA clone from rice endosperm polyadenylated RNA was obtained and used as a hybridization probe. Northern blots showed that ADPglucose pyrophosphorylase mRNA was slightly larger in leaf (2100 bases) than in endosperm tissue (1900 bases). These studies indicated that in cereals there are at least two tissue specific forms of ADPglucose pyrophosphorylase that are encoded by distinct mRNA transcripts. Analysis of genomic DNA by Southern blotting suggested that ADPglucose pyrophosphorylase is encoded by a small gene family.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Anderson C. W., Straus J. W., Dudock B. S. Preparation of a cell-free protein-synthesizing system from wheat germ. Methods Enzymol. 1983;101:635–644. doi: 10.1016/0076-6879(83)01044-7. [DOI] [PubMed] [Google Scholar]
- Aoyagi K., Bassham J. A. Pyruvate orthophosphate dikinase mRNA organ specificity in wheat and maize. Plant Physiol. 1984 Sep;76(1):278–280. doi: 10.1104/pp.76.1.278. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
- Copeland L., Preiss J. Purification of Spinach Leaf ADPglucose Pyrophosphorylase. Plant Physiol. 1981 Nov;68(5):996–1001. doi: 10.1104/pp.68.5.996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fuchs R. L., Smith J. D. The purification and characterization of ADP-glucose pyrophosphorylase A from developing maize seeds. Biochim Biophys Acta. 1979 Jan 12;566(1):40–48. doi: 10.1016/0005-2744(79)90246-8. [DOI] [PubMed] [Google Scholar]
- Kislev N., Rubenstein I. Utility of ethidium bromide in the extraction from whole plants of high molecular weight maize DNA. Plant Physiol. 1980 Dec;66(6):1140–1143. doi: 10.1104/pp.66.6.1140. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lizardi P. M. Methods for the preparation of messenger RNA. Methods Enzymol. 1983;96:24–38. doi: 10.1016/s0076-6879(83)96006-8. [DOI] [PubMed] [Google Scholar]
- Sowokinos J. R., Preiss J. Pyrophosphorylases in Solanum tuberosum: III. PURIFICATION, PHYSICAL, AND CATALYTIC PROPERTIES OF ADPGLUCOSE PYROPHOSPHORYLASE IN POTATOES. Plant Physiol. 1982 Jun;69(6):1459–1466. doi: 10.1104/pp.69.6.1459. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]