Ptr1 evolved convergently with RPS2 and Mr5 to mediate recognition of AvrRpt2 in diverse solanaceous species.

The Ptr1 (Pseudomonas tomato race 1) locus in Solanum lycopersicoides confers resistance to strains of Pseudomonas syringae pv. tomato expressing AvrRpt2 and Ralstonia pseudosolanacearum expressing RipBN. Here we describe the identification and phylogenetic analysis of the Ptr1 gene. A single recombinant among 585 F2 plants segregating for the Ptr1 locus was discovered that narrowed the Ptr1 candidates to eight nucleotide-binding leucine-rich repeat protein (NLR)-encoding genes. From analysis of the gene models in the S. lycopersicoides genome sequence and RNA-Seq data, two of the eight genes emerged as the strongest candidates for Ptr1. One of these two candidates was found to encode Ptr1 based on its ability to mediate recognition of AvrRpt2 and RipBN when it was transiently expressed with these effectors in leaves of Nicotiana glutinosa. The ortholog of Ptr1 in tomato and in Solanum pennellii is a pseudogene. However, a functional Ptr1 ortholog exists in Nicotiana benthamiana and potato, and both mediate recognition of AvrRpt2 and RipBN. In apple and Arabidopsis, recognition of AvrRpt2 is mediated by the Mr5 and RPS2 proteins, respectively. Phylogenetic analysis places Ptr1 in a distinct clade compared with Mr5 and RPS2, and it therefore appears to have arisen by convergent evolution for recognition of AvrRpt2.

Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts--implications for thylakoid formation and photosystem II maintenance.

The chloroplast ATP-dependent metalloprotease FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II (PSII) from photoinhibition, and, apparently, the formation of thylakoids. In Arabidopsis, it is encoded by a family of 12 genes. However, the products of only four of them, FtsH1, 2, 5 and 8, have been found in chloroplasts to date. Mutations in two of these, FtsH2 and 5, demonstrate a visible phenotype of variegated leaves, with the phenotype of the FtsH2 mutant being more pronounced. Moreover, the degree of variegation appears to be dependent on developmental stage and environmental factors, suggesting an intricate relationship between the different gene products. To explore this, developmental and light effects on the accumulation of FtsH protease were studied in wild-type (WT) and FtsH2-mutant plants. Whereas cotyledons of the mutant were indistinguishable from those of the WT, the first true leaves were almost completely white. Subsequent leaves contained increasing proportions of green sectors. Analysis of the mRNA of the four FtsH genes, in cotyledons, first and second leaves of WT and mutant plants, revealed that: (i) transcript level increases during development, and (ii) transcript level in the mutant is higher than in the WT. FtsH protein level in the mutant was ca. 50% of that found in the WT, whereas the levels of other thylakoid proteins were the same. In individual leaves, the level of FtsH protein increased during development as well. Exposure of seedlings to different light intensities did not affect the degree of variegation, suggesting that it is due to a defect in chloroplast development rather than photobleaching. Examination of FtsH protein during exposure to high light revealed a decrease in its level, concomitant with a decrease in PSII potential, suggesting that the kinetics of photoinhibition reflects not only photodamage to PSII and induction of protective mechanisms, but also a decrease in repair capacity due to a reduction in the level of FtsH protease.