Identification and characterization of a novel calcineurin-binding protein in scallop testis.
Calcineurin has been inferred to function in meiosis and spermiogenesis in testis. Here, we identified a calcineurin-binding protein in scallop testis by Far-Western blot analysis using purified calcineurin as a probe. The molecular mass of the binding protein estimated on the blot was 75 kDa. The isolated cDNA clone encoded a novel 474-residue protein, named CaNBP75. The region between T6 and A210 of CaNBP75 was responsible for the interaction with calcineurin. CaNBP75 was predominantly expressed in testis and ovary of scallop. Thus, CaNBP75 may modulate the physiological function of calcineurin in the testis and ovary of scallop, such as in spermiogenesis or meiosis.
Nakatomi
Akiko
A
Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Yazawa
Michio
M
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D026481:Blotting, Far-Western; D019703:Calcineurin / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics* / Q000302:isolation & purification*; D018076:DNA, Complementary; D005260:Female; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008974:Mollusca; D010053:Ovary / Q000737:chemistry; D011485:Protein Binding; D016415:Sequence Alignment; D013737:Testis / Q000737:chemistry*
D002352:Carrier Proteins; D018076:DNA, Complementary; D019703:Calcineurin