Abstract
Leucine-rich repeat receptor-like kinases (LRR-RLKs) represent the largest subfamily of receptor-like kinases (RLKs) and play important roles in regulating growth, development, and stress responses in plants. In this study, 246 LRR-RLK genes were identified in the potato (Solanum tuberosum) genome, which were further classified into 14 subfamilies. Gene structure analysis revealed that genes within the same subgroup shared similar exon/intron structures. A signature small peptide recognition motif (RxR) was found to be largely conserved within members of subfamily IX, suggesting that these members may recognize peptide signals as ligands. 26 of the 246 StLRR-RLK genes were found to have arisen from tandem or segmental duplication events. Expression profiling revealed that StLRR-RLK genes were differentially expressed in various organs/tissues, and several genes were found to be responsive to different stress treatments. Furthermore, StLRR-RLK117 was found to be able to form homodimers and heterodimers with StLRR-RLK042 and StLRR-RLK052. Notably, the overlapping expression region of StLRR-RLK117 with Solanum tuberosum WUSCHEL (StWUS) suggested that the CLV3–CLV1/BAM–WUS feedback loop may be conserved in potato to maintain stem cell homeostasis within the shoot apical meristem.
Highlights
Unlike animals, the static build of plants handicaps their ability to escape from the hazards of environmental fluctuations
All LRR-receptor-like kinases (RLKs) full-length amino acid sequences in Arabidopsis were downloaded from TAIR and these sequences were used as queries to perform a BLASTP search against the potato protein database with an E-value cutoff of 0.01
StLRR-RLK042 and StLRR-RLK052 were grouped with AtBAM1 and AtBAM2, these results indicated that potato CLAVATA 1 (CLV1) and BAMs may interact with each other, and StLRR-RLK117 could form homodimers in regulating stem cell homeostasis in the shoot apical meristem (SAM)
Summary
The static build of plants handicaps their ability to escape from the hazards of environmental fluctuations. Lacking this essential survival ability, plants have been provided with unique cell surface receptor proteins that allow the plants to perform cell-to-cell communication and to interact with their environment. In plants, these cellular receptors are known as receptor-like kinases (RLKs) which generally comprise an extracellular ligand binding domain, a transmembrane domain, and an intercellular cytoplasmic kinase domain. The structural feature of RLK proteins demonstrates a high degree of divergence
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