June
1998
, Volume
11
, Number
6
Pages
572
-
576
Authors
Ying-Tsu
Loh
,
Jianmin
Zhou
,
and
Gregory B.
Martin
Affiliations
Department of Agronomy, 1150 Lilly Hall of Life Sciences, Purdue University, West Lafayette, IN 47907-1150, U.S.A.
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RelatedArticle
Accepted 14 February 1998.
Abstract
The tomato Pto kinase confers resistance to bacterial speck disease caused by strains of Pseudomonas syringae pv. tomato that express the avirulence gene avrPto. Pto contains a putative myristylation site at its amino terminus that was hypothesized to play a role in localizing Pto in the plant cell. Site-directed mutagenesis was used to change the invariant glycine residue in the myristylation motif to an alanine. Transgenes encoding the mutant Pto(G2A) and wild-type Pto were placed behind the cauliflower mosaic virus 35S promoter and transformed into tomato plants that are susceptible to bacterial speck disease. Both the mutant and wild-type forms of Pto conferred resistance to a strain of P. syringae pv. tomato expressing avrPto. These results indicate that the myristylation motif of Pto is not required for bacterial speck disease resistance.
JnArticleKeywords
Additional keywords:
Fen,
signal transduction,
tyrosine kinase.
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ArticleCopyright
© 1998 The American Phytopathological Society