A novel regulatory function of selenocysteine lyase, a unique catalyst to modulate major urinary protein |
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Authors: | Mi-Sun Kwak Hisaaki Mihara Nobuyoshi Esaki |
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Affiliation: | Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan |
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Abstract: | Mouse selenocysteine lyase (SCL) catalyzes the decomposition of -selenocysteine into -alanine and selenium with pyridoxal 5′-phosphate as a coenzyme. When using SCL as bait in a yeast two-hybrid screening method, major urinary protein I (MUP-I) was identified as a protein that interacts with SCL. This interaction was confirmed with an in vitro binding assay. MUP-I is known as a pheromone-binding protein that accommodates volatile effectors to affect the physiology and behavior of mice. We found that the binding of 2-naphthol to MUP-I was significantly inhibited by SCL, suggesting that SCL regulates the binding capacity of MUP-I. |
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Keywords: | Selenium Selenocysteine lyase Major urinary protein Yeast two-hybrid screening Protein–protein interaction |
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