NH2-terminal amino acid sequences of precursor and mature forms of the ribulose-1,5-bisphosphate carboxylase small subunit from Chlamydomonas reinhardtii.
A precursor (pS) to the small subunit (S) of ribulose1-,5-bisphosphate carboxylase is the major product of cell-free protein synthesis directed by poly(A) containing RNA from Chlamydomonas reinhardtii. We present sequence data for in vitro-synthesized pS, for in vitro-synthesized S that in generated from pS by posttranslational incubation with a Chlamydomonas cell extract, and for in vitro-synthesized, mature S. We show that pS contains an NH2-terminal extension of 44 amino acid residues that is removed by cleavage at the correct site when pS is converted to S by an endoprotease present in the Chlamydomonas cell extract.
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000032:analysis*; D002696:Chlamydomonas / Q000201:enzymology*; D004792:Enzyme Precursors / Q000032:analysis* / Q000096:biosynthesis; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase / Q000032:analysis* / Q000096:biosynthesis
D004792:Enzyme Precursors; D002262:Carboxy-Lyases; D012273:Ribulose-Bisphosphate Carboxylase