J. Biol. Chem., Vol. 261, Issue 24, 11124-11130, Aug, 1986
Gene structure, protein structure, and regulation of the synthesis of a sulfur-rich protein in pea seeds
TJ Higgins, PM Chandler, PJ Randall, D Spencer, LR Beach, RJ Blagrove, AA Kortt and AS Inglis
Two low molecular weight pea seed albumins (Mr approximately 6000 and
approximately 4000) have been characterized by protein, cDNA, and gene
sequencing. Both proteins are encoded by separate regions of the same mRNA
species. The initial translation product is a preproprotein from which a
signal sequence is removed co-translationally. The resultant proprotein
(PA1) is then cleaved post-translationally to yield the mature form of the
two albumins (PA1a and PA1b). Comparison of cDNA and protein sequences
suggests that at least four different PA1 genes are expressed in the pea
genome. Both PA1a and PA1b have an unusually high cysteine content (7.5 and
16.2%, respectively). Pea seeds developing under suboptimal levels of
sulfur nutrient supply contain reduced levels of PA1 mRNA and accumulate
greatly reduced levels of PA1a and PA1b in the mature seed. In vitro
transcription studies showed that this reduced level of PA1 mRNA resulted
from reduced post- transcriptional stability rather than an altered rate of
transcription of the PA1 gene. In contrast, during normal seed development,
the level of PA1 mRNA seems to be under transcriptional control. Sequence
comparisons reveal some homology between PA1 and a number of low molecular
weight proteins from seeds of a wide range of mono- and dicotyledonous
plants.