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

التفاصيل البيبلوغرافية
العنوان: Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109.
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.)
References: Ozhogina OA, Trexler M, Bányai L, Llinás M and Patthy L (2001) Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family identify the kringle domain of neurotrypsin as a potential link between FN2 domains and kringles. Prot Sci 10, 2114-2122.
Patthy L, Trexler M, Vali Z, Banyai L and Váradi A (1984) Kringles: modules specialized for protein binding homology of the gelatin-binding region of fibronectin with the kringle structures of proteases. FEBS Lett 171, 131-136.
Baker ME (1985) The PDC-109 protein from bovine seminal plasma is similar to the gelatin-binding domain of bovine fibronectin and kringle domain of human tissue-type plasminogen activator. Biochem Biophys Res Commun 3, 1010-1014.
Constantine KL, Madrid M, Bányai L, Trexler M, Patthy L and Llinás M (1992) Refined solution structure and ligand-binding properties of PDC-109 domain b. J Mol Biol 223, 281-298.
Bányai L, Tordai J and Patthy L (1994) The gelatin binding site of human 72 kDa type IV collagenase. Biochem J 298, 403-407.
Pickford AR, Potts JR, Bright JR, Phan I and Campbell ID (1997) Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin binding domain. Structure 5, 359-370.
Sticht H, Pickford AR, Potts JR and Campbell ID (1998) Solution structure of the glycosylated second type 2 module of fibronectin. J Mol Biol 276, 177-187.
Napper CE, Drickamer K and Taylor ME (2006) Collagen binding by the mannose receptor mediated through the fibronectin type II domain. Biochem J 395, 579-586.
Esch FS, Ling NC, Böhlen P, Ying SY and Guillemin R (1983) Primary structure of PDC-109, a major protein constituent of bovine seminal plasma. Biochem Biophys Res Commun 113, 861-867.
Desnoyers L and Manjunath P (1992) Major proteins of bovine seminal plasma exhibit novel interactions with phospholipids. J Biol Chem 267, 10149-10155.
Ramakrishnan M, Anbazhagan V, Pratap TV, Marsh D and Swamy MJ (2001) Membrane insertion and lipid-protein interactions of bovine seminal plasma protein, PDC-109 investigated by spin label electron spin resonance spectroscopy. Biophys J 81, 2215-2225.
Swamy MJ (2004) Interaction of bovine seminal plasma proteins with model membranes and sperm plasma membranes. Curr Sci 87, 203-211.
Wah DA, Tornero CF, Sanz L, Romero A and Calvete JJ (2002) Sperm coating mechanism from the 1.8Å crystal structure of PDC-109-phosphorylcholine complex. Structure 10, 505-514.
Gasset M, Magdaleno L and Calvete JJ (2000) Biophysical study of the perturbation of the model membranes caused by seminal plasma protein PDC-109. Arch Biochem Biophys 374, 241-247.
Thomas CJ, Anbazhagan V, Ramakrishnan M, Sultan N, Surolia I and Swamy MJ (2003) Mechanism of membrane binding by the bovine seminal plasma protein, PDC-109. A surface plasmon resonance study. Biophys J 84, 3037-3044.
Anbazhagan V, Sankhala RS, Singh BP and Swamy MJ (2011) Thermodynamics of interaction of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes. An isothermal titration calorimetric study, PLoS ONE 6, e25993.
Sankhala RS and Swamy MJ (2010) The major protein of bovine seminal plasma, PDC-109, is a molecular chaperone. Biochemistry 49, 3908-3918.
Sankhala RS, Damai RS and Swamy MJ (2011) Correlation of membrane binding and hydrophobicity to the chaperone-like activity of PDC-109. PLoS ONE 6, e17330.
Sankhala RS, Kumar CS, Singh BP, Arangasamy A and Swamy MJ (2012) HSP-1/2, a major protein of equine seminal plasma, exhibits chaperone-like activity. Biochem Biophys Res Commun 427, 18-23.
Kumar CS and Swamy MJ (2016) A pH switch regulates the inverse relationship between membranolytic and chaperone-like activities of HSP-1/2, a major protein of horse seminal plasma. Biochemistry 55, 3650-3657.
Kumar CS, Singh BP, Alim S and Swamy MJ (2018) Factors influencing the chaperone-like activity of major proteins of mammalian seminal plasma, equine HSP-1/2 and bovine PDC-109. Effect of membrane binding, pH and ionic strength. Adv Exp Med Biol 1112, 53-68.
Singh BP, Saha I, Nandi I and Swamy MJ (2017) Spermine and spermidine act as chemical chaperones and enhance chaperone-like and membranolytic activities of bovine seminal plasma protein, PDC-109. Biochem Biophys Res Commun 493, 1418-1424.
Singh BP, Sankhala RS, Asthana A, Ramakrishna T, Rao ChM and Swamy MJ (2019) Glycosylation differentially modulates membrane-destabilizing and chaperone-like activities of PDC-109, the major protein of bovine seminal plasma. Biochem Biophys Res Commun 511, 28-34.
Lefebvre J, Fan J, Chevalier S, Sullivan R, Carmona E and Manjunath P (2007) Genomic structure and tissue-specific expression of human and mouse genes encoding homologues of the major bovine seminal plasma proteins. Mol Hum Reprod 13, 45-53.
Lefebvre J, Boileau G and Manjunath P (2009) Recombinant expression and affinity purification of a novel epididymal human sperm-binding protein, BSPH1. Mol Hum Reprod 15, 105-114.
Calvete JJ, Varela PF, Sanz L, Romero A, Mann K and Töpfer-Petersen E (1996) A procedure for the large-scale isolation of major bovine seminal plasma proteins. Protein Expr Purif 8, 48-56.
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
Gasset M, Saiz JL, Sanz L, Gentzel M, Töpfer-Petersen E and Calvete JJ (1997) Conformational features and thermal stability of bovine seminal plasma protein PDC-109 oligomers and phosphorylcholine-bound complexes. Eur J Biochem 250, 735-744.
Damai RS, Sankhala RS, Anbazhagan V and Swamy MJ (2010) Destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109: 31P-NMR and AFM studies. IUBMB Life 62, 841-851.
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
Moreau R, Thérien I, Lazure C and Manjunath P (1998) Type II domains of BSP-A1/-A2 proteins: binding properties, lipid efflux and sperm capacitation potential. Biochem Biophys Res Commun 246, 148-154.
Damai RS, Anbazhagan V and Swamy MJ (2009) Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes. Biochim Biophys Acta 1794, 1725-1733.
De Petro G, Barlati S, Vartio T and Vaheri A (1981) Transformation-enhancing activity of gelatine-binding fragments of fibronectin. Proc Natl Acad Sci USA 78, 4965-4969.
Atkin KE, Brentnall AS, Harris G, Bingham RJ, Erat MC, Millard CJ, Schwarz-Linek U, Staunton D, Vakonakis I, Campbell ID and et al (2010) The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules. J Biol Chem 285, 36977-36983.
Larson CL, Samuelson DR, Eucker TP, O'Loughlin JL and Konkel ME (2013) The fibronectin-binding motif within FlpA facilitates Campylobacter jejuni adherence to host cell and activation of host cell signaling. Emerg Microbes Infect 2, e65.
Singh D, Raman B, Ramakrishna T and Rao ChM (2006) The cataract-causing mutation G98R in human αA-crystallin leads to folding defects and loss of chaperone activity. Mol Vis 12, 1372-1379.
Koteiche HA and Mchaourab HS (2006) Mechanism of a hereditary cataract phenotype. Mutations in αA-crystallin activate substrate binding. J Biol Chem 281, 14273-14279.
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
الوصف
تدمد:1873-3468
DOI:10.1002/1873-3468.13617