| Literature DB >> 8038606 |
Abstract
From a pollen tube cDNA library of Petunia inflata, we isolated clones encoding a protein with structural features and biochemical properties characteristic of receptor-like kinases. It was designated PRK1 for pollen receptor-like kinase 1. The cytoplasmic domain of PRK1 is highly similar to the kinase domains of other plant receptor-like kinases and contains nearly all of the conserved amino acids for serine/threonine kinases. The extracellular domain of PRK1 contains leucine-rich repeats as found in some other plant receptor-like kinases, but overall its sequence in this region does not share significant similarity. Characterization of a gene encoding PRK1 revealed the presence of two introns. During pollen development, PRK1 mRNA was first detected in anthers containing mostly binucleate microspores; it reached the highest level of mature pollen and remained at a high level in in vitro-germinated pollen tubes. The recombinant cytoplasmic domain of PRK1 autophosphorylated on serine and tyrosine, suggesting that PRK1 may be a dual-specificity kinase. Monospecific immune serum to the recombinant extracellular domain of PRK1 detected a 69-kD protein in microsomal membranes of pollen and pollen tubes. The characteristics of PRK1 suggest that it may play a role in signal transduction events during pollen development and/or pollination.Entities:
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Year: 1994 PMID: 8038606 PMCID: PMC160470 DOI: 10.1105/tpc.6.5.709
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277