J. Biol. Chem., Vol. 260, Issue 30, 16162-16168, 12, 1985
The Euglena gracilis chloroplast ribulose-1,5-bisphosphate carboxylase gene. II. The spliced mRNA and its product
JC Gingrich and RB Hallick
The polypeptide product of the gene for the large subunit of ribulose-
1,5-bisphosphate carboxylase from Euglena gracilis based on the DNA
sequence of the chloroplast-encoded gene is described. The large subunit
polypeptide of 475 codons is co-linear with the homologous polypeptides
from other chloroplasts and cyanobacteria. The amino acid sequence is 92%
homologous to that of Chlamydomonas, 84% homologous to spinach, 82%
homologous to maize, and 80% homologous to that of the cyanobacterium
Anabaena variabilis. Known functional domains of the protein are coded by
the larger exons of the gene. Introns in the gene generally occur at coding
sequences specifying hydrophilic, presumably surface exposed, regions of
the polypeptide. The location of some of the introns may reflect a
separation of functional domains. The 5'- and 3'-ends of the rbcL
transcript were determined by primer extension sequencing using reverse
transcriptase and S1 nuclease protection, respectively. The transcribed but
untranslated sequences are quite distinct from those from other rbcL loci.
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