科研之友
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摘要
We have isolated a 1.6 kb clone from a cDNA library made from the olfactory rosettes of the Atlantic salmon (Salmo salar). The clone contains a 1200 bp, open reading frame (named OSC) which codes for a protein with 400 amino-acid residues (Oscp). The mRNA corresponding to OSC is strongly expressed in the olfactory rosettes and weakly expressed in gills but is expressed in only these two tissues. This suggests that Oscp may have a specific and important role in olfaction. The sequence of Oscp suggests that it is not globular. Predictions show only a small fraction of alpha-helix. Oscp is hydrophilic but with the number of positively charged residues equal to the number of negatively charged residues. No closely similar protein can be found on the basis of homology searches or hydrophobicity comparisons. However, a 44 residue segment (G300 through K343) is significantly homologous to a segment of alpha-lactalbumin (G51 through K94). The similarities include the 19 residues of the "alpha-lactalbumin-lysozyme C signature," the ten residues of the Ca2+ binding elbow and the four cysteine residues which provide two key disulfide links in alpha-lactalbumin and lysozyme C. Two more Cys residues are also very similarly placed. We conclude that the gene OSC codes for a unique protein which most likely contains a specific site for binding Ca2+ and plays a unique role in the signal pathway of olfaction in salmon.
- 出版日期2002-2
