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, AUG 27-31, 2000, GATERSLEBEN, GERMANY.

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Abstract

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
ISSN:	0176-1617
Date:	April 2001
Volume:	158
Number:	4
Number of Pages:	5
Page Range:	pp. 499-503
Publication Status:	Published
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
URI:	http://wrap.warwick.ac.uk/id/eprint/12235

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