Plant Physiology Preview
Published on February 24, 2002; 10.1104/pp.010519
Received June 14, 2001
Returned for revision July 22, 2001
Accepted August 29, 2001
Identification, Purification, and Molecular Cloning of
N-1-Naphthylphthalmic Acid-Binding Plasma Membrane-Associated
Aminopeptidases from Arabidopsis
Angus S. Murphy *, Karen R. Hoogner , Wendy Ann Peer , and Lincoln Taiz
Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana 47907--1165 (A.S.M., W.A.P.); and Molecular, Cellular and Developmental Biology Department, University of California, Santa Cruz, California 95064 (K.R.H., L.T.)
* Corresponding author; email: amurphy{at}hort.purdue.edu.
Polar transport of the plant hormone auxin is regulated at the cellular level by inhibition of efflux from a plasma membrane (PM) carrier. Binding of the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA) to a regulatory site associated with the carrier has been characterized, but the NPA-binding protein(s) have not been identified. Experimental disparities between levels of high-affinity NPA binding and auxin transport inhibition can be explained by the presence of a low-affinity binding site and in vivo hydrolysis of NPA. In Arabidopsis, colocalization of NPA amidase and aminopeptidase (AP) activities, inhibition of auxin transport by artificial ß-naphthylamide substrates, and saturable displacement of NPA by the AP inhibitor bestatin suggest that PM APs may be involved in both low-affinity NPA binding and hydrolysis. We report the purification and molecular cloning of NPA-binding PM APs and associated proteins from Arabidopsis. This is the first report of PM APs in plants. PM proteins were purified by gel permeation, anion exchange, and NPA affinity chromatography monitored for tyrosine-AP activity. Lower affinity fractions contained two orthologs of mammalian APs involved in signal transduction and cell surface-extracellular matrix interactions. AtAPM1 and ATAPP1 have substrate specificities and inhibitor sensitivities similar to their mammalian orthologs, and have temporal and spatial expression patterns consistent with previous in planta histochemical data. Copurifying proteins suggest that the APs interact with secreted cell surface and cell wall proline-rich proteins. AtAPM1 and AtAPP1 are encoded by single genes. In vitro translation products of ATAPM1 and AtAPP1 have enzymatic activities similar to those of native proteins.
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