Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone‐like activities of bovine seminal plasma protein PDC‐109
2020
Singh, Bhanu P. | Asthana, Abhishek | Basu, Amrita | Tangirala, Ramakrishna | Mohan Rao, Chintalagiri | Swamy, Musti J.
The fibronectin type II (FnII) domain, present in diverse vertebrate proteins, plays crucial roles in several fundamental biological processes. PDC‐109, the major bovine seminal plasma protein, contains two FnII domains that bind to choline phospholipids on sperm plasma membrane and induce lipid efflux crucial for successful fertilization. PDC‐109 also exhibits chaperone‐like activity and protects other proteins against various types of stress. Here, we show that a core tryptophan residue is highly conserved across species in the FnII domains. Mutation of conserved tryptophan residues W47, W93, and W106 in the FnII domains of PDC‐109 to alanine leads to drastic decrease or complete abolition of membrane‐binding and chaperone‐like activities. These observations suggest that conserved tryptophans are important for the function of FnII proteins.
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