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PLANT PHYSIOLOGY , Vol 114, Issue 1 345-352, Copyright © 1997 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
A Defective Signal Peptide Tethers the floury-2 Zein to the Endoplasmic Reticulum Membrane
J. W. Gillikin, F. Zhang, C. E. Coleman, H. W. Bass, B. A. Larkins and R. S. Boston
Department of Botany, North Carolina State University, Raleigh, North Carolina 27695 (J.W.G., F.Z., H.W.B., R.S.B.)
The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a
general decrease in storage protein synthesis, altered protein body
morphology, and the synthesis of a novel 24-kD [alpha]-zein storage
protein. Unlike storage proteins in normal kernels and the majority of
storage proteins in fl2 kernels, the 24-kD [alpha]-zein contains a signal
peptide that would normally be removed during protein synthesis and
processing. The expected processing site of this [alpha]-zein reveals a
putative mutation alaine->valine (Ala->Val) that is not found at
other junctions between signal sequences and mature proteins. To
investigate the impact of such a mutation on signal peptide cleavage, we
have assayed the 24-kD fl2 [alpha]-zein in a co-translational processing
system in vitro. Translation of RNA from fl2 kernels or synthetic RNA
encoding the fl2 [alpha]-zein in the presence of microsomes yielded a 24-kD
polypeptide. A normal signal peptide sequence, generated by site-directed
mutagenesis, restored the capacity of the RNA to direct synthesis of a
properly processed protein in a cell-free system. Both the fl2 [alpha]-zein
and the fl2 [alpha]-zein (Val->Ala) were translocated into the lumen of
the endoplasmic reticulum. The processed fl2 [alpha]-zein (Val->Ala) was
localized in the soluble portion of the microsomes, whereas the fl2
[alpha]-zein co-fractionated with the microsomal membranes. By remaining
anchored to protein body membranes during endosperm maturation, the fl2
zein may thus constrain storage protein packing and perturb protein body
morphology.
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