Dimer structure of a neuropeptide precursor established: consequences for processing.
A prohormone (P1) of locust adipokinetic hormone I (AKH I) is shown here to be a homodimer of a 41 residue subunit called the A-chain. The A-chain, from the N terminal, consists of AKH I (10 amino acids starting with pyroglutamate) followed by a Gly-Lys-Arg processing site and then a 28 residues called the alpha chain containing a single cysteine and a potential Arg-Lys processing site. When processed each molecule of the homodimer precursor yields two copies of AKH I and one alpha chain homodimer. We call the alpha-alpha homodimer product of P1 processing AKH precursor related peptide 1 or APRP 1. The Arg-Lys dibasic pair found within the alpha chain is not cleaved in vivo. Our results show that neuropeptide precursors can be dimers and that dimer products can be synthesized by processing of a preformed dimer precursor rather than by dimerization of independent subunits.
Hekimi
S
S
University of Geneva, Laboratoire de Neurobiologie, Switzerland.
Burkhart
W
W
Moyer
M
M
Fowler
E
E
O'Shea
M
M
D000595:Amino Acid Sequence; D000818:Animals; D006110:Grasshoppers / Q000235:genetics / Q000378:metabolism*; D007301:Insect Hormones / Q000096:biosynthesis* / Q000235:genetics; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000096:biosynthesis* / Q000235:genetics; D011498:Protein Precursors / Q000235:genetics* / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D007301:Insect Hormones; D009479:Neuropeptides; D011498:Protein Precursors; C014956:adipokinetic hormone (locust)