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N-terminal Sequence Analysis of Bovine Dentin Phosphophoryn after Conversion of Phosphoseryl to S-propylcysteinyl Residues
N.L. Huq
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
K.J. Cross
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
G.H. Talbo
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
P.F. Riley
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
A. Loganathan
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
M.A. Crossley
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
J.W. Perich
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
E.C. Reynolds
Oral Health Science Unit, School of Dental Science, The University of Melbourne, 711 Elizabeth Street, Melbourne, Victoria, 3000, Australia
Bovine dentin phosphophoryn (BDP), a protein rich in aspartyl (Asp) and O-phosphoseryl (Ser[P]) residues, is synthesized by odontoblasts and is believed to be involved in matrix-mediated biomineralization of dentin. We have purified BDP, using selective precipitation and ion exchange chromatography, from an EDTA soluble dentin extract and converted the Ser(P) residues to S-propylcysteinyl residues that are stable to Edman degradation, facilitating the determination of the amino acid sequence of the N-terminal 38 residues. After the initial Asp-Ser(P)-Pro-Asn-Ser( P)-Ser(P)-Asp-Glu-Ser(P)-Asn-Gly-, the sequence contained the repeated motifs Asp-Ser(P) and Asp-Ser(P)-Ser(P). Purified BDP migrated as a single band on gradient SDS-PAGE with an apparent molecular weight of 156 kDa. This value was consistent with the molecular weight of the dephosphorylated protein of 105 kDa determined by means of MALDI mass spectrometry.
Key Words: bovine dentin phosphophoryn • sequence analysis.
REFERENCES
- Adamson NJ, Reynolds EC (1995a). Characterization of multiply phosphorylated peptides selectively precipitated from a pancreatic casein digest. J Dairy Sci 78:2653-2659.[Abstract]
- Adamson NJ, Reynolds EC (1995b). Characterisation of tryptic casein phosphopeptides prepared under industrially-relevant conditions. Biotech Bioeng 45:196-204.
- Butler WT, Bhown M., DiMuzio MT, Cothran WC, Linde A. (1983). Multiple forms of rat dentin phosphoproteins. Arch Biochem Biophys 225:178-186.[CrossRef][Medline]
[Order article via Infotrieve]
- Debruyne I. (1983). Staining of alkali-labile phosphoproteins and alkaline phosphatases on polyacrylamide gels. Anal Biochem 133:110-115.[Medline]
[Order article via Infotrieve]
- Evans JS, Chan SI ( 1994). Phosphophoryn, a biomineralization template protein: pH dependent protein folding experiments. Biopolymers 34:507-527.[CrossRef][Medline]
[Order article via Infotrieve]
- Evans JS, Chan SI, editors (1991). The N-terminal fragment of bovine phosphophoryn, an extracellular mineral matrix protein, shares sequence homology with viral, bacterial and eukaryotic transcriptional and post-translational regulatory proteins. In: Proteins: structure, dynamics, design. Leiden, The Netherlands: ESCOM.
- Feng JQ, Luan X., Wallace J., Jing D., Ohshima T., Kulkarni AB, et al. (1998). Genomic organization, chromosomal mapping, and promoter analysis of the mouse dentin sialophosphoprotein (Dspp) gene, which codes for both dentin sialoprotein and dentin phosphoprotein. J Biol Chem 273:9457-9464.[Abstract/Free Full Text]
- Garnier J., Robson B. (1989). The GOR method for predicting secondary structures in proteins. In: Prediction of protein structure and the principles of protein conformation. Fasman G, editor. New York: Plenum, pp. 417-465.
- George A., Bannon L., Sabsay B., Dillon JW, Malone J., Veis A., et al. (1996). The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process. J Biol Chem 271:32869-32873.[Abstract/Free Full Text]
- George A., Srinivasan R., Thotakura S., Veis A. ( 1998). The phosphophoryn gene family: identical domain structures at the carboxyl end. Eur J Oral Sci 106:221-226.
- Hames BD (1990). Gel electrophoresis of proteins. In: The practical approach. Rickwood D, Hames BD, editors. Oxford: IRL Press, pp. 53-57.
- Jonsson M., Fredriksson A. (1978). Isoelectric focusing of the phosphoprotein of rat-incisor dentin in ampholine and acid pH gradients. Evidence for carrier ampholyte-protein complexes. J Chromatogr 157:234-242.[Medline]
[Order article via Infotrieve]
- Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.[CrossRef][Medline]
[Order article via Infotrieve]
- MacDougall M., Zeichner-David M., Slavkin HC (1985). Production and characterization of antibodies against murine dentine phosphoprotein. Biochem J232:493-500.
- Meyer HE, Hoffmann-Posorske E., Heilmeyer Lmg Jr (1991). Protein phosphorylation B. Methods in enzymology. Vol. 201. Hunter T, Sefton BM, editors. New York: Academic Press, pp. 169-185.
- Perich JW, Meggio F., Reynolds EC, Marin 0, Pinna LA (1992). Roles of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1. Biochemistry 31:5893-5897.
- Pinna LA, Meggio F., Marchiori F. (1990). Peptides and protein phosphorylation. Boca Raton, FL: CRC Press.
- Prevelige JP, Fasman G. (1989). Chou-Fasman prediction of the secondary structure of proteins: The Chou-Fasman-Prevelige algorithm. In: Prediction of protein structure and the principles of protein conformation. Fasman G, editor. New York: Plenum, pp. 391-416.
- Reynolds EC, Riley PF, Adamson NJ (1994). A selective precipitation purification procedure for multiple phosphoseryl-containing peptides and methods for their identification. Anal Biochem 217:277-284.[CrossRef][Medline]
[Order article via Infotrieve]
- Ritchie HH, Wang LH ( 1996). Sequence determination of an extremely acidic rat dentin phosphoprotein. J Biol Chem 271:21695-21698.[Abstract/Free Full Text]
- Ritchie HH, Ritchie DG, Wang LH ( 1998). Six decades of dentinogenesis research. Historical and prospective views on phosphophoryn and dentin sialoprotein. Eur J Oral Sci 106:211-220.
- Sabsay B., Stetler-Stevenson WG, Lechner JH, Veis A. ( 1991). Domain structure and sequence distribution in dentin phosphophoryn. Biochem J 276:699-707.
- Small D., Chou PY, Fasman GD (1977). Occurrence of phosphorylated residues in predicted P-turns. Implications for β-turns participation in control mechanisms. Biochem Biophys Res Commun 79:341-346.[Medline]
[Order article via Infotrieve]
- Stetler-Stevenson WG, Veis A. ( 1983). Bovine dentin phosphophoryn: composition and molecular weight. Biochemistry 22:4326-4335.
- Swiderek K., Jaquet K., Meyer HE, Heilmeyer LM Jr (1988). Cardiac troponin I, isolated from bovine heart, contains two adjacent phosphoserines. A first example of phosphoserine determination by derivatization to S-ethylcysteine. Eur J Biochem 176:335-342.[Medline]
[Order article via Infotrieve]
- Weinstock M., Leblond CP (1973). Radioautographic visualization of the deposition of a phosphoprotein at the mineralization front in the dentin of the rat incisor. J Cell Biol 56:838-845.[Free Full Text]
- Wilmot CM, Thornton JM (1988). Analysis and prediction of the different types of beta-turn in proteins. J Mol Biol 203:221-232.[CrossRef][Medline]
[Order article via Infotrieve]
- Wilmot CM, Thomton JM (1990). Beta-turns and their distortions: a proposed new nomenclature. Protein Eng 3:479-493.[Abstract/Free Full Text]
Journal of Dental Research, Vol. 79, No. 11,
1914-1919 (2000)
DOI: 10.1177/00220345000790111701
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