دورية أكاديمية
Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109.
العنوان: | Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109. |
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المؤلفون: | Singh BP; School of Chemistry, University of Hyderabad, India., Asthana A; Centre for Cellular and Molecular Biology, Hyderabad, India., Basu A; School of Chemistry, University of Hyderabad, India., Tangirala R; Centre for Cellular and Molecular Biology, Hyderabad, India., Mohan Rao C; Centre for Cellular and Molecular Biology, Hyderabad, India., Swamy MJ; School of Chemistry, University of Hyderabad, India. |
المصدر: | FEBS letters [FEBS Lett] 2020 Feb; Vol. 594 (3), pp. 509-518. Date of Electronic Publication: 2019 Oct 09. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE |
أسماء مطبوعة: | Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd. Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies. |
مواضيع طبية MeSH: | Conserved Sequence* , Tryptophan*, Cell Membrane/*metabolism , Seminal Vesicle Secretory Proteins/*chemistry , Seminal Vesicle Secretory Proteins/*metabolism, Amino Acid Sequence ; Animals ; Cattle ; Ligands ; Models, Molecular ; Mutation ; Protein Domains ; Protein Multimerization ; Protein Structure, Quaternary ; Seminal Vesicle Secretory Proteins/genetics |
مستخلص: | 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. (© 2019 Federation of European Biochemical Societies.) |
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فهرسة مساهمة: | Keywords: capacitation; cholesterol efflux; fibronectin type II domain; lipid-protein interaction; molecular chaperone; mutational analysis |
المشرفين على المادة: | 0 (Ligands) 0 (Seminal Vesicle Secretory Proteins) 0 (seminal vesicle secretory protein 109, Bos taurus) 8DUH1N11BX (Tryptophan) |
تواريخ الأحداث: | Date Created: 20190926 Date Completed: 20201007 Latest Revision: 20201007 |
رمز التحديث: | 20240628 |
DOI: | 10.1002/1873-3468.13617 |
PMID: | 31552690 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1873-3468 |
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DOI: | 10.1002/1873-3468.13617 |