1. Predicted Amino Acid Sequence of the Tomato Cf-4 Protein (Thomas et al
Predicted Amino Acid Sequence of the Tomato Cf-4 Protein (Thomas et al., 1997).Structural domains A to G of Cf-4 (Jones and Jones, 1997) are indicated at left.
Predicted Amino Acid Sequence of the Tomato Cf-4 Protein (Thomas et al., 1997).Structural domains A to G of Cf-4 (Jones and Jones, 1997) are indicated at left. Cf-4 LRRs within domains C1 and C3 that are common to Cf-4 and Cf-9 are numbered in black at right, LRRs specific to Cf-4 are shown in blue, and the corresponding Cf-9 LRRs are shown in parentheses in red. The amino acids that distinguish Cf-4 from Cf-9 are shown in blue, and deleted amino acids relative to Cf-9 are indicated by black dots. Sequences that form part of the putative β-strand/β-turn structural motif in LRR proteins (Kobe and Deisenhofer, 1994; Jones and Jones, 1997) are delimited by vertical lines. The consensus sequence for plant extracellular LRRs is shown boxed below the amino acid sequence, and consensus residues with a possible β-strand configuration are shown in red. The location of restriction enzyme sites that facilitated the construction of Cf-4/Cf-9 chimeras also are shown. Sites in Cf-4DS and Cf-9DS genomic clones for ClaI, BglII, HindIII, and PvuII (indicated at right) are represented by yellow boxes outlined in black. Restriction sites for EcoRI and HindIII in sequences encoding LRRs 13 and 19 of Cf-4 and LRRs 15 and 21 of Cf-9, respectively, are indicated as green boxes.
Brande B. H. Wulff et al. Plant Cell 2001;13:
©2001 by American Society of Plant Biologists