Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109

FEBS Letters

article

Bhanu P. Singh¹  Abhishek Asthana²  Amrita Basu¹  Ramakrishna Tangirala²  Chintalagiri Mohan Rao²  Musti J. Swamy¹ 

[1] School of Chemistry, University of Hyderabad;Centre for Cellular and Molecular Biology

关键词: capacitation;    cholesterol efflux;    fibronectin type II domain;    lipid-protein interaction;    molecular chaperone;    mutational analysis;   

DOI  :  10.1002/1873-3468.13617

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown