scholarly journals Protein Synthesis in Cotyledons of Pisum sativum L

1972 ◽  
Vol 49 (4) ◽  
pp. 476-481 ◽  
Author(s):  
Leonard Beevers ◽  
Rozanne Poulson
Keyword(s):  
Protein Synthesis ◽  
Pisum Sativum ◽  
Pisum Sativum L

scholarly journals Protein synthesis in the cotyledons of Pisum sativum L. Protein factors involved in the binding of phenylalanyl-transfer ribonucleic acid to ribosomes*

1974 ◽  
Vol 139 (1) ◽  
pp. 61-69 ◽  
Author(s):  
Gary N. Wells ◽  
Leonard Beevers
Keyword(s):  
Protein Synthesis ◽  
Complex Formation ◽  
Pisum Sativum ◽  
Ribonucleic Acid ◽  
Ternary Complex ◽  
Supernatant Fraction ◽  
Soluble Factors ◽  
Pisum Sativum L ◽  
Sensitive Site ◽  
Millipore Filters

1. Proteinaceous factors contained in a 0.5m-KCl extract of ribosomes from pea cotyledons form a ternary complex at 0°C with [14C]phenylalanyl-tRNA and poly(U). The complex is measured by its quantitative retention on Millipore filters. 2. Complex-assembly is optimal at 5mm-Mg2+ and is independent of GTP and ribosomes. 3. The addition of ribosomes is required to stabilize the complex at 34°C. The complex binds to a puromycin-sensitive site on the ribosome. 4. Soluble factors from the 250000g supernatant of pea cotyledon form a Millipore-retainable complex dependent on GTP and ribosomes. 5. Complex-formation by soluble factors has a Mg2+ optimum of 10–12mm and forms a puromycin-insensitive complex with ribosomes. 6. The function of the ribosomal protein factors and the supernatant fraction in initiation of protein synthesis is discussed.

Long-lived Messenger RNA and its Relationship to Protein Synthesis During Germination of Pea (Pisum sativum L.) Seeds

1986 ◽  
Vol 57 (6) ◽  
pp. 771-781 ◽  
Author(s):  
S. C. Greenway ◽  
G. M. Strangeway ◽  
D. Grierson ◽  
J. A. Bryant
Keyword(s):  
Protein Synthesis ◽  
Pisum Sativum ◽  
Messenger Rna ◽  
Pisum Sativum L

scholarly journals EFFECTS OF 60COBALT IONIZING IRRADIATION ON GROWTH AND POLYSOME CONTENT IN PISUM SATIVUM L. `ALASKA'

HortScience ◽  
1992 ◽  
Vol 27 (12) ◽  
pp. 1261d-1261
Author(s):  
Jody A. Goodrich
Keyword(s):  
Protein Synthesis ◽  
Pisum Sativum ◽  
Plant Cells ◽  
Root Tip ◽  
Nuclear Accidents ◽  
Ionizing Irradiation ◽  
Pisum Sativum L ◽  
Living Organisms ◽  
Injurious Effects

This research tested the hypothesis that 60Co ionizing irradiation degrades polysomes to monosomes, a process that reduces growth of Pisum sativum seedlings. Dry and imbibed seeds and 5-day-old seedlings were exposed to 1.8, 3.6, 7.2, 14.4, or 28.8 krad of 60Co irradiation. Immediately after irradiation treatments, dry and imbibed seeds were planted, and later seedlings were harvested and analyzed. Five 1-cm root-tip samples from 5-day-old seedlings were crushed and layered onto 15% to 60% sucrose gradients and centrifuged for 55 min. The samples were processed through an ISCO ultraviolet chart maker. The monosome and polysome weights were read and analyzed. The monosome content was greater in the irradiated 5-day-old seedlings than in seedlings from dry and imbibed seeds. The growth of 5-day-old irradiated seedlings and seedlings from imbibed seeds was less than that of seedlings from dry seeds. The reduced growth of the irradiated seedlings suggests damage to the polysomes. When protein synthesis in plant cells is altered, perhaps through RNA decoding mechanisms, growth may be partially or completely arrested. Using sensitive plants to establish the injurious effects of ionizing irradiation on living organisms can educate and alert society to the detrimental effects of overexposure to irradiation such as that caused by nuclear accidents.

scholarly journals Control of storage-protein synthesis during seed development in pea (Pisum sativum L.)

1982 ◽  
Vol 208 (1) ◽  
pp. 119-127 ◽  
Author(s):  
J A Gatehouse ◽  
I M Evans ◽  
D Bown ◽  
R R D Croy ◽  
D Boulter
Keyword(s):  
Protein Synthesis ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Sodium Dodecyl ◽  
Northern Hybridization ◽  
Transcriptional Level ◽  
Stages Of Development ◽  
Tissue Specific ◽  
Mrna Species ◽  
Pisum Sativum L

The tissue-specific syntheses of seed storage proteins in the cotyledons of developing pea (Pisum sativum L.) seeds have been demonstrated by estimates of their qualitative and quantitative accumulation by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and rocket immunoelectrophoresis respectively. Vicilin-fraction proteins initially accumulated faster than legumin, but whereas legumin was accumulated throughout development, different components of the vicilin fraction had their predominant periods of synthesis at different stages of development. The translation products in vitro of polysomes isolated from cotyledons at different stages of development reflected the synthesis in vivo of storage-protein polypeptides at corresponding times. The levels of storage-protein mRNA species during development were estimated by ‘Northern’ hybridization using cloned complementary-DNA probes. This technique showed that the levels of legumin and vicilin (47000-Mr precursors) mRNA species increased and decreased in agreement with estimated rates of synthesis of the respective polypeptides. The relative amounts of these messages, estimated by kinetic hybridization were also consistent. Legumin mRNA was present in leaf poly(A)+ RNA at less than one-thousandth of the level in cotyledon poly(A)+ (polyadenylated) RNA, demonstrating tissue-specific expression. Evidence is presented that storage-protein mRNA species are relatively long-lived, and it is suggested that storage-protein synthesis is regulated primarily at the transcriptional level.

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