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THE PLANT CELL, Vol 6, Issue 3 393-404, Copyright © 1994 by American Society of Plant Biologists
A Higher Plant Extracellular Vitronectin-like Adhesion Protein Is Related to the Translational Elongation Factor-1[alpha]
J. K. Zhu, B. Damsz, A. K. Kononowicz, R. A. Bressan and P. M. Hasegawa
Center for Plant Environmental Stress Physiology, Purdue University, 1165 Horticulture Building, West Lafayette, Indiana 47907-l165
Higher plant proteins immunologically related to the animal substrate
adhesion molecule vitronectin have recently been observed and implicated in
a variety of biological processes, such as plasma membrane-cell wall
adhesion, pollen tube extension, and bacterium-plant interaction. We
provide evidence that, similar to vitronectin, one of these proteins, PVN1
(plant vitronectin-like 1), isolated from 428 mM NaCl-adapted tobacco cells
binds to glass surfaces and heparin. PVN1 was isolated by glass bead
affinity chromatography. Isolated PVN1 has adhesive activity based on
results from a baby hamster kidney cell-spreading assay. This plant
adhesion protein was detected in all tissues examined but was most abundant
in roots and salt-adapted cultured cells. Immunogold labeling indicated
that PVN1 is localized in the cell wall of cortical and transmitting tissue
cells of pollinated mature styles. A partial amino acid sequence of PVN1
revealed no similarity with vitronectin but, instead, was nearly identical
to the translational elongation factor-1[alpha] (EF-1[alpha]). A clone
isolated by screening a tobacco cDNA expression library with anti-PVN1
encoded a protein with greater than 93% identity to sequences of
EF-1[alpha] from plants of numerous species. Immunological cross-reactivity
between tobacco PVN1 and EF-1[alpha] as well as the reaction between the
EF-1[alpha] antibody and the 65- and 75-kD vitronectin-like proteins of a
fucoidal alga supported the conclusion that the plant extracellular
adhesion protein PVN1 is related to EF-1[alpha].
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