Bovine β-lactoglobulin: Interaction studies with palmitic acid

Protein Science

Volumn 9, Issue 7, 2000, Pages 1347-1356

  Ragona, Laura ^a   Fogolari, Federico ^b   Zetta, Lucia ^a   Pérez, Dolores M ^c   Puyol, Pilar ^c   De Kruif, Kees ^d   Löhr, Frank ^e   Rüterjans, Heinz ^e   Molinari, Henriette ^b  

^a Laboratorio NMR   (Italy)

^b UNIVERSITY OF VERONA   (Italy)

^c Lab Genet Bioquim Grupos S   (Spain)

^d NIZO FOOD RESEARCH   (Netherlands)

^e GOETHE UNIVERSITY   (Germany)

Author keywords

Bovine lactoglobulin; Lipocalin binding sites; Nuclear magnetic resonance; Palmitic acid; T1 measurements; Tanford transition

Indexed keywords

BETA LACTOGLOBULIN; CARBON 13; HYDROGEN; PALMITIC ACID;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; LIGAND BINDING; LIPID ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION;

EID: 0033862274     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1347     Document Type: Article

References (65)

1. Antosiewicz J, McCammon JA, Gilson MK. 1994. Prediction of pH-dependent properties of proteins. J Mol Biol 238:317-330.
2. Bartels C, Xia T, Billeter M, Guntert P, Wüthrich K. 1995. The program XE-ASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 5:1-10.
3. Bax A, Subramanian S. 1986. Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy. J Magn Reson 67:565-569.
4. Brownlow S, Morais Cabral JH, Cooper R, Flower DR, Yewdall SJ, Polikarpov I, North ACT, Sawyer L. 1997. Bovine β-lactoglobulin at 1.8 Å resolution -Still an enigmatic lipocalin. Structure 5:481-495.
5. Bychkova VE, Berni R, Rossi GL, Kutyshenko VP, Ptitsyn OB. 1992. Retinol-binding is in the molten globule state at low pH. Biochemistry 31:7566-7571.
6. 13C NMR study. J Biol Chem 264:2700-2710.
7. Cistola DP, Small DM, Hamilton JA. 1987. Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. J Biol Chem 262:10971-10979.
8. Creamer LK. 1995. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 34:7170-7176.
9. 13C]-γ-ionones bound to β-lactoglobulin B. Pharmaceutical Res 16:651-659.
10. Dufour E, Genot C, Haertlé T. 1994. β-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy. Biochim Biophys Acta 1205:105-112.
11. Flower DR. 1995. Multiple molecular recognition properties of the lipocalin protein family. J Mol Recognition 8:185-195.
12. Fogolari F, Ragona L, Licciardi S, Romagnoli S, Michelutti R, Ugolini R, Molinari H. 2000. Electrostatic properties of bovine β-lactoglobulin. Proteins Struct Funct Genet 39:317-330.
13. Fogolari F, Ragona L, Zetta L, Romagnoli S, De Kruif KG, Molinari H. 1998. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett 436:149-154.
14. Frapin D, Dufour E, Haertlé T. 1993. Pobing the fatty acid binding site of β-lactoglobulins. J Protein Chem 12:443-449.
15. Glasgow BJ, Gasymov OK, Abduragimov AR, Yusifov TN, Altenbach C, Hubbell WL. 1999. Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labelling. Biochemistry 38:3707-13716.
16. Hamdan M, Curcuruto O, Molinari H, Zetta L, Ragona L. 1996. Monitoring complexation between some proteins and naphthalene dye by electrospray mass spectrometry. J Mass Spectroscopy 31:1261-1264.
17. Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y. 1999. Solution structure and dynamics of bovine beta-lactoglobulin A. Protein Sci 8:2541-2545.
18. Lange DC, Kothari R, Patel RC, Patel SC. 1998. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys Chem 74:45-51.
19. Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Rüterjans H. 1995. Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multi-dimensional NMR spectroscopy. Eur J Biochem 230:266-280.
20. 15N NMR study of Gramicidin S in water and organic solvents. J Am Chem Soc 106:1939-1941.
21. Madura JD, Briggs JM, Wade RC, Davis ME, Luty BA, Ilin A, Antosiewicz J, Gilson MK, Bagheri B, Scott LR, et al. 1995. Electrostatic and diffusion of molecules in solution: Simulations with the University of Houston brownian dynamics program. Comp Phys Comm 91:57-95.
22. Mesgarzadeh A, Pfeiffer S, Engelke J, Lassen D, Rüterjans H. 1998. Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy. Eur J Biochem 251:781-786.
23. Molinari H, Esposito G, Consonni R, Pegna M, Zetta L. 1992. Distance evaluation by means of heteronuclear SQC-NOESY experiments. J Biomol NMR 2:289-299.
24. Molinari H, Ragona L, Varani L, Musco G, Consonni R, Zetta L, Monaco HL. 1996. Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Lett 381:237-243.
25. Narayan M, Berliner LJ. 1997. Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 36:1906-1911.
26. Narayan M, Berliner LJ. 1998. Mapping fatty acid binding to β-lactoglobulin: Ligand binding is restricted by modification of Cys 121. Protein Sci 7:150-157.
27. 13C NMR study. J Biol Chem 15:9262-9269.
28. Pérez MD, Calvo M. 1995. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review. J Diary Sci 78:978-988.
29. Pérez MD, Diaz de Villegas C, Sanchez L, Aranda P, Ena JM, Calvo M. 1989. Interaction of fatty acids with β-lactoglobulin and albumin from ruminant milk. J Biochem 106:1094-1097.
30. Pérez MD, Sanchez L, Aranda P, Ena JM, Oria R, Calvo M. 1991. Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk. Biochim Biophys Acta 1123:151-155.
31. Puyol P, Pérez MD, Ena JM, Calvo M. 1991. Interaction of bovine b-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids. Agric Biol Chem 55:2515-2520.
32. Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB. 1999. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci 8:75-83.
33. Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB. 1998a. Structural basis of the tanford transition of bovine β-lactoglobulin. Biochemistry 37:14014-14023.
34. Qin BY, Creamer LK, Baker EN, Jameson GB. 1998b. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett 438:272-278.
35. Ragona L, Fogolari F, Romagnoli S, Zetta L, Maubois JL, Molinari H. 1999. Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements. J Mol Biol 293:953-969.
36. Ragona L, Pusterla F, Zetta L, Monaco HL, Molinari H. 1997. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Fold Des 2:281-290.
37. Richieri GV, Ogata RT, Kleinfeld AM. 1996. Kinetics of fatty acid interactions with fatty acid binding proteins from adipocyte, heart and intestine. J Biol Chem 271:11291-11300.
38. Scapin G, Gorgon JI, Sacchettini JC. 1992. Refinement of the structure of recombinant rat intestinal fatty acid-binding protein. J Biol Chem 267:4253-4269.
39. Tanford C, Nozaki Y. 1959. Physico-chemical comparison of β-lactoglobulins A and B. J Biol Chem 234:2874-2877.
40. Uhrinova S, Smith M, Jameson GB, Uhrin D, Sawyer L, Barlow PN. 2000. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 39:3567-3574.
41. 15N chemical shifts for bovine β-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unforded form. J Biomol NMR 12:89-107.
42. Woolf TB. 1998. Simulations of fatty acid-binding proteins suggests sites important for function. I. Stearic acid. Biophys J 74:681-693.
43. Wu SY, Pérez MD, Puyol P, Sawyer L. 1999. β-Lactoglobulin binds palmitate within its central cavity. J Biol Chem 274:170-174.
44. Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC. 1994. Structural studies on human muscle fatty acid binding protein at 1.4 Å resolution: Binding with three C18 fatty acids. Structure 2:523-534.
45. Milligan G, Parenti M, Magee AI. 1995. The dynamic role of palmitoylation in signal transduction. TIBS 20:181-186.
46. S. Eur J Biochem 257:236-241.
47. O'Brien PJ, St. Jules RS, Reddy TS, Bazan NG, Zatz M. 1987. Acylation of disc membrane rhodopsin may be nonenzymatic. J Biol Chem 262:5210-5215.
48. Omary MB, Trowbridge IS. 1981. Biosynthesis of the human transferrin receptor in cultured cells. J Biol Chem 256:12888-12892.
49. Parente A, Merrifield B, Geraci G, D'Alessio G. 1985. Molecular basis of superreactivity of cysteine residues 31 and 32 of seminal ribonuclease. Biochemistry 24:1098-1104.
50. Quesnel S, Silvius JR. 1994. Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-coA-dependent acylation at the lipid bilayer interface. Biochemistry 33:13340-13348.
51. Phelps KK, Walker RA. 2000. NEM tubulin inhibits minus end assembly by a reversible cap. Biochemistry 39:3877-3885.
52. Resh MD. 1999. Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta 145:1-18.
53. Sackett DL, Bhattacharyya B, Wolff J. 1994. Local unfolding and the stepwise loss of the functional properties of tubulin. Biochemistry 33:12868-12878.
54. Snyder GH, Cennerazzo MJ, Karalis AJ, Field D. 1981. Electrostatic influence of local cysteine environments on disulfide exchange kinetics. Biochemistry 20:6509-6519.
55. Snyder GH, Reddy MK, Cennerazzo MJ, Field D. 1983. Use of local electrostatic environments of cysteines to enhance formation of a desired species in a reversible disulfide exchange reaction. Biochim Biophys Acta 749:219-226.
56. Stephens RE. 1984. Membrane tubulin. Biol Cell 57:95-110.
57. O stimulation by GAP-43. EMBO J 11:2095-2102.
58. Tao N, Wagner SJ, Lublin DM. 1996. CD36 is palmitoylated on both N-and C-terminal cytoplasmic tails. J Biol Chem 271:22315-22320.
59. Veil M, Sachs K, Heckelman M, Maretzki D, Hofmann KP, Schmidt MFG. 1998. Palmitoylation of rhodopsin with S-protein acyl transferase: Enzyme catalysed reaction versus autocatalytic acylation. Biochim Biophys Acta 1394:90-98.
60. Weimbs T, Stoffel W. 1992. Proteolipid protein (PLP) of CNS myelin: Positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Biochemistry 31:12289-12296.
61. Wilson L. 1975. Microtubules as drug receptors: Pharmacological properties of microtubule protein. Ann NY Acad Sci 253:213-231.
62. Wolff J, Knipling L, Sackett DL. 1996b. Charge-shielding and the "paradoxical" stimulation of tubulin polymerization by guanidine hydrochloride. Biochemistry 35:5910-5920.
63. Wolff J, Sackett DL, Knipling L. 1996a. Cation selective promotion of tubulin polymerization by alkali metal chlorides. Protein Sci 5:2020-2028.
64. Yamashita A, Watanabe M, Tonegawa T, Sugiura T, Waku K. 1995. Acyl-coA binding and acylation of UDP-glucuronyl transferase. Biochem J 312:301-308.
65. Zambito AM, Wolff J. 1997. Palmitoylation of tubulin. Biochem Biophys Res Commun 239:650-654.