The C-terminal tetrapeptide of phaseolin is sufficient to target green fluorescent protein to the vacuole
UNSPECIFIED (2001) The C-terminal tetrapeptide of phaseolin is sufficient to target green fluorescent protein to the vacuole. In: 8th International Symposium on Plant Seeds/5th Gatersleben Research Conference, GATERSLEBEN, GERMANY, AUG 27-31, 2000. Published in: JOURNAL OF PLANT PHYSIOLOGY, 158 (4). pp. 499-503.Full text not available from this repository.
Phaseolin is a vacuolar storage glycoprotein synthesized as a precursor with a short C-terminal propeptide. We have recently shown that deletion of the last four C-terminal amino acids (AFVY, which are part of, or constitute the propeptide) abolishes vacuolar targeting, causing phaseolin to be secreted. Here we provide biochemical and microscopical evidence that the AFVY tetrapeptide, when fused to a secreted version of green fluorescent protein (GFP), inhibits GFP secretion and leads to its accumulation in vacuoles, where it is processed. This demonstrates that the tetrapeptide contains sufficient information for vacuolar sorting.
|Item Type:||Conference Item (UNSPECIFIED)|
|Subjects:||S Agriculture > SB Plant culture|
|Journal or Publication Title:||JOURNAL OF PLANT PHYSIOLOGY|
|Publisher:||URBAN & FISCHER VERLAG|
|Official Date:||April 2001|
|Number of Pages:||5|
|Page Range:||pp. 499-503|
|Title of Event:||8th International Symposium on Plant Seeds/5th Gatersleben Research Conference|
|Location of Event:||GATERSLEBEN, GERMANY|
|Date(s) of Event:||AUG 27-31, 2000|
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