The present article reports on the characterization of ScBAK1, a leucine-rich repeat receptor-like kinase from sugarcane (
Saccharum spp.), expressed predominantly in bundle-sheath cells of the mature leaf and potentially involved in cellular signaling cascades
mediated by high levels of sugar in this organ. In this report, it was shown that the ScBAK1 sequence was similar to the brassinosteroid
insensitive1-associated receptor kinase1 (BAK1). The putative cytoplasmatic domain of ScBAK1 contains all the amino acids
characteristic of protein kinases, and the extracellular domain contains five leucine-rich repeats and a putative leucine
zipper. Transcripts of ScBAK1 were almost undetectable in sugarcane roots or in any other sink tissue, but accumulated abundantly
in the mature leaves. The ScBAK1 expression was higher in the higher sugar content individuals from a population segregating
for sugar content throughout the growing season. In situ hybridization in sugarcane leaves showed that the ScBAK1 mRNA accumulated
at much higher levels in bundle-sheath cells than in mesophyll cells. In addition, using biolistic bombardment of onion epidermal
cells, it was shown that ScBAK1-GFP fusions were localized in the plasma membrane as predicted for a receptor kinase. All
together, the present data indicate that ScBAK1 might be a receptor involved in the regulation of specific processes in bundle-sheath
cells and in sucrose synthesis in mature sugarcane leaves.
Keywords Brassinosteroid signaling - Functional analysis - Receptor-like kinases -
Saccharum
- Signal transduction
Communicated by J. Register.
Renato Vicentini and Juliana de Maria Felix contributed equally to this work.