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PLANT PHYSIOLOGY , Vol 114, Issue 3 863-870, Copyright © 1997 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
The N-Terminal Propeptide of the Precursor to Sporamin Acts as a Vacuole-Targeting Signal even at the C Terminus of the Mature Part in Tobacco Cells
Y. Koide, H. Hirano, K. Matsuoka and K. Nakamura
Laboratory of Biochemistry, School of Agricultural Sciences, Nagoya University, Chikusa, Nagoya 464-01, Japan (Y.K., H.H., K.M., K.N.)
An asparagine-proline-isoleucine-arginine-leucine (NPIRL) and its related
sequences in the N-terminal propeptides (NTPP) of several plant vacuolar
proteins, including that of sporamin from sweet potato (SPO) function as
vacuole-targeting determinants in a manner that is distinct from the
vacuole-targeting determinant in the CTPPs of other plant vacuolar
proteins. When the mutant precursor to sporamin, SPO-NTPP (in which NTPP
was moved to the C terminus of the mature part), was expressed in tobacco
(Nicotiana tabacum) cells, the pro-form was efficiently targeted to the
vacuole and the NTPP was cleaved off. Unlike the results obtained with the
wild-type precursor, substitution of the NPIRL sequence in the C-terminally
located NTPP to asparagine-proline-glycine-arginine-leucine in the
SPO-isoleucine-28-to-glycine mutant resulted in missorting of less than 20%
of the pro-form to the medium. Unlike the vacuolar transport of SPO-NTPP,
the vacuolar transport of SPO-isoleucine-28-to-glycine was strongly
inhibited by 33 [mu]M wortmannin, which is similar to the C-terminal
propeptide-mediated vacuolar transport. These results suggest that the
vacuole-targeting function of the NPIRL sequence is not strictly dependent
on its location at the N terminus of a protein and that the C-terminally
located mutant NTPP acquired some physicochemical properties of the
C-terminal vacuole-targeting sequence.
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