Abstract
In addition to the marked reduction in legumin synthesis and legumin mRNA levels reported earlier (Chandler, Higgins, Randall, Spencer 1983 Plant Physiol 71: 47-54), pulse labeling of S-deficient Pisum sativum L. seeds showed that a high relative level of total vicilin (vicilin plus convicilin) synthesis was maintained throughout the entire phase of protein accumulation, whereas in nondeficient seeds vicilin synthesis is largely confined to the first half of this phase. Fractionation of pulse-labeled proteins on Na-dodecylsulfate-polyacrylamide gels showed that the synthesis of the Mr 50,000 family of vicilin polypeptides was increased and greatly extended in S-deficient seeds whereas that of convicilin was slightly reduced. Other changes apparent from pulse-labeling experiments include a depression, to different degrees, in the synthesis of three major albumin polypeptides.
The level of the mRNAs for seven major seed proteins was followed throughout development of control and sulfur-deficient seeds. In all cases, the changes in each mRNA closely reflected the pattern of synthesis of its corresponding polypeptide seen by pulse labeling. S-deficient seeds showed an elevated level of Mr 50,000 vicilin mRNA which remained high throughout seed formation, whereas legumin mRNA levels were greatly reduced at all stages of development.
When S-deficient plants were given an adequate supply of sulfate midway through seed development, there was a shift toward the protein synthesis profile characteristic of healthy plants. The synthesis of legumin and two albumins rapidly increased and the synthesis of Mr 50,000 vicilin declined more slowly. Similar responses were seen in detached, S-deficient seeds supplied directly with adequate sulfate.
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- Chandler P. M., Higgins T. J., Randall P. J., Spencer D. Regulation of Legumin Levels in Developing Pea Seeds under Conditions of Sulfur Deficiency: Rates of Legumin Synthesis and Levels of Legumin mRNA. Plant Physiol. 1983 Jan;71(1):47–54. doi: 10.1104/pp.71.1.47. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chandler P. M. The use of single-stranded phage DNAs in hybrid arrest and release translation. Anal Biochem. 1982 Nov 15;127(1):9–16. doi: 10.1016/0003-2697(82)90137-3. [DOI] [PubMed] [Google Scholar]
- Chrispeels M. J., Higgins T. J., Spencer D. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J Cell Biol. 1982 May;93(2):306–313. doi: 10.1083/jcb.93.2.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gatehouse J. A., Lycett G. W., Croy R. R., Boulter D. The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.). Biochem J. 1982 Dec 1;207(3):629–632. doi: 10.1042/bj2070629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Higgins T. J., Chandler P. M., Zurawski G., Button S. C., Spencer D. The biosynthesis and primary structure of pea seed lectin. J Biol Chem. 1983 Aug 10;258(15):9544–9549. [PubMed] [Google Scholar]
- Lycett G. W., Delauney A. J., Gatehouse J. A., Gilroy J., Croy R. R., Boulter D. The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding sequence for preprovicilin. Nucleic Acids Res. 1983 Apr 25;11(8):2367–2380. doi: 10.1093/nar/11.8.2367. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schroeder H. E. Major albumins of Pisum cotyledons. J Sci Food Agric. 1984 Feb;35(2):191–198. doi: 10.1002/jsfa.2740350210. [DOI] [PubMed] [Google Scholar]
- Spencer D., Higgins T. J., Button S. C., Davey R. A. Pulse-labeling Studies on Protein Synthesis in Developing Pea Seeds and Evidence of a Precursor Form of Legumin Small Subunit. Plant Physiol. 1980 Sep;66(3):510–515. doi: 10.1104/pp.66.3.510. [DOI] [PMC free article] [PubMed] [Google Scholar]