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(Received for publication, March 4, 1996, and in revised form, July 25, 1996)
From the Department of Botany and Plant Sciences and Graduate
Genetics Group, University of California,
Riverside, California 92521-0124
Leucine aminopeptidase (LAP) is induced by
wounding and bacterial pathogen infection in tomato. DNA blot analysis
of XbaI-digested
Volume 271, Number 42,
Issue of October 18, 1996
pp. 25880-25887
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
lap genomic clones
demonstrated that LapA1 and LapA2 cDNAs
were encoded by two different LapA genes in the tomato
genome. The coding and untranslated regions of LapA1 and
LapA2 mRNAs shared more than 93% identity. The deduced
amino acid sequences of LapA cDNA clones and in
vitro translation of LapA1 mRNA indicated that
LAP-A was synthesized as a 60-kDa precursor protein. The processing of
a 60-kDa preLAP-A into the mature 55-kDa LAP-A was demonstrated
in vivo by expression of the full-length LapA1
cDNA in insect cells. Sequencing of a single LAP-A form
isolated from a two-dimensional polyacrylamide gel indicated that LAP-A
proteins had two different N termini that were separated by two
residues. The LAP-A presequence had features similar to chloroplast
transit peptides. Comparison of LAP-A levels in chloroplast and total
protein extracts from methyl jasmonate-treated leaves indicated that a
small proportion of the LAP-A proteins was detected in the plastids.
Inspection of the LAP-A presequence indicated the presence of a dibasic
protease (Kex2/furin) processing site motif 6-8 residues upstream from
the LAP-A N termini. Its potential role in LAP-A precursor biogenesis
is discussed.
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