Regulation of the transcription of storage-protein mRNA in nuclei isolated from developing pea (Pisum sativum L.) cotyledons

Planta ◽  
1984 ◽  
Vol 160 (6) ◽  
pp. 559-568 ◽  
Author(s):  
I. Marta Evans ◽  
John A. Gatehouse ◽  
Ronald R. D. Croy ◽  
Donald Boulter
Heredity ◽  
1984 ◽  
Vol 53 (1) ◽  
pp. 185-191 ◽  
Author(s):  
Sayed H Mahmoud ◽  
John A Gatehouse

1985 ◽  
Vol 232 (1) ◽  
pp. 261-265 ◽  
Author(s):  
I M Evans ◽  
J A Gatehouse ◽  
D Boulter

The effects of sulphur deficiency on the expression of storage-protein genes in developing pea (Pisum sativum) cotyledons were studied. Legumin-gene transcription was decreased by S-deficiency, but not to the same extent as the decrease in the level of legumin mRNA. Vicilin-gene transcription was not significantly affected. Control of gene expression may thus occur during transcription and/or post-transcriptional events.


Planta ◽  
1980 ◽  
Vol 148 (1) ◽  
pp. 49-56 ◽  
Author(s):  
Ronald R. D. Croy ◽  
John A. Gatehouse ◽  
I. Marta Evans ◽  
Donald Boulter

1992 ◽  
Vol 40 (2) ◽  
pp. 200-205 ◽  
Author(s):  
Alain. Baniel ◽  
Daniele. Caer ◽  
Bernard. Colas ◽  
Jacques. Gueguen

Planta ◽  
1980 ◽  
Vol 148 (1) ◽  
pp. 57-63 ◽  
Author(s):  
Ronald R. D. Croy ◽  
John A. Gatehouse ◽  
I. Marta Evans ◽  
Donald Boulter

1980 ◽  
Vol 191 (2) ◽  
pp. 509-516 ◽  
Author(s):  
R R Croy ◽  
J A Gatehouse ◽  
M Tyler ◽  
D Boulter

A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named ‘convicilin’ and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.


Planta ◽  
1979 ◽  
Vol 144 (5) ◽  
pp. 455-462 ◽  
Author(s):  
I. Marta Evans ◽  
Ronald R. D. Croy ◽  
Philippa Hutchinson ◽  
Donald Boulter ◽  
Peter I. Payne ◽  
...  

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