Characterization of p26olf, a novel calcium-binding protein in the frog olfactory epithelium.
We have previously shown that p26olf is a novel S100-like Ca(2+)-binding protein in the frog olfactory epithelium. In this paper, we characterized the Ca(2+) binding property of p26olf, examined the precise localization in the frog olfactory epithelium, and searched for the possible target proteins of p26olf. By flow dialysis experiments using (45)Ca, p26olf was suggested to bind approximately 4 Ca(2+). Circular dichroism measurement showed that binding of Ca(2+) to p26olf induces an increase in the apparent content of both alpha-helix and beta-sheet with an apparent K(d) value of 2.4 micrometer. Electron microscopic observation disclosed p26olf immunoreactivity in the cilia, dendritic knob, and dendrite of olfactory receptor cells. Blot overlay analysis and affinity purification of p26olf-binding proteins showed that p26olf binds to a frog beta-adrenergic receptor kinase-like protein in a Ca(2+)-dependent manner. These results suggested that p26olf has some roles in the olfactory transduction or adaptation.
Miwa
N
N
Department of Biology, Graduate School of Science, Osaka University, Machikane-yama 1-1, Toyonaka, Osaka 560-0043, Japan. nmiwa@bio.sci.osaka-u.ac.jp
Uebi
T
T
Kawamura
S
S
D029845:Amphibian Proteins; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D007150:Immunohistochemistry; D009831:Olfactory Mucosa / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011892:Rana catesbeiana; D009418:S100 Proteins / Q000737:chemistry / Q000378:metabolism*; D051552:beta-Adrenergic Receptor Kinases
D029845:Amphibian Proteins; D002135:Calcium-Binding Proteins; C115659:P26OLF protein, Rana catesbeiana; D009418:S100 Proteins; D017868:Cyclic AMP-Dependent Protein Kinases; D051552:beta-Adrenergic Receptor Kinases