Abstract
The gene 5 product of bacteriophage fd is a small DNA binding protein of 9,800 daltons containing 87 amino acids (Alberts et al. 1972; Oey and Knippers 1972). Its primary physiological role is the stabilization and protection of the single-strand DNA daughter virions from duplex formation following replication in the host (Salstrom and Pratt 1971). Because of the highly cooperative nature of its binding to DNA, it has the capacity to unwind or destabilize native DNA. Under low ionic strength conditions in vitro, it will melt double-stranded homopolymers and will reduce the melting temperature of native double-strand calf thymus DNA by 40°C (Salstrom and Pratt 1971).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Alberts B, Frey L, Delius H (1972) Isolation and characterization of gene 5 protein of filamentous bacterial viruses. J Mol Biol 68: 139–152
Anderson RA, Nakashima Y, Coleman JE (1975) Chemical modifications of functional residues of fd gene 5 DNA-binding protein. Biochemistry 14: 907–917
Cavalieri S, Goldthwait DA, Neet K (1976) The isolation of a dimer of gene 9 protein of bacteriophage fd. J Mol Biol 102: 713–722
Coleman JE, Armitage IM (1980) Biochemistry (in press)
Coleman JE, Anderson RA, Ratcliffe RG, Armitage IM (1976) Structure of gene 5 protein-oligo-dexynucleotide complexes as determined by H, F and P nuclear magnetic resonance. Biochemistry 15: 5419–5430
Cuypers T, van der Oudera FJ, DeJong WW (1974) The amino acid sequence of gene 5 protein of bacteriophage M 13. Biochem Biophys Res Commun 59: 557–563
Day LA (1973) Circular dichroism and ultra-violet absorption of a deoyribonucleic acid binding protein of filamentous bacteriophage. Biochemistry 12: 5329–5339
Dunker AK, Anderson EA (1975) The binding of the fd gene-5 protein to single-stranded nucleic acid. Biochim Biophys Acta 402: 31–34
McPherson A, Molineux I, Rich A (1976) Crystalization of a DNA unwinding protein: Preliminary X-ray analysis of fd bacteriophage gene-5 product. J Mol Biol 106: 1077–1081
McPherson A, Jurnak FA, Wang AH-J, Molineux I, Rich A (1979) Structure at 2.3 Åresolution of the gene 5 product of bacteriophage fd: A DNA unwinding protein. J Mol Biol 134: 379–400
Nakashima Y, Dunker AK, Marion DA, Konigsberg W (1974) The amino acid sequence of a DNA binding protein, the gene 5 product of fd filamentous bacteriophage. FEBS Lett 40: 290–292
Oey JL, Knippers R (1972) Properties of the isolated gene-5 protein of bacteriophage fd. J Mol Biol 68: 125–128
Pratt D, Laws P, Griffity J (1974) Complex of bacteriophage M 13 single-stranded DNA and gene 5 protein. J Mol Biol 82: 425–439
Pretorius HT, Klein M, Day LA (1975) Gene V protein of fd bacteriophage. Dinner formation and the role of tyrosyl groups in DNA binding. J Biol Chem 250: 9262–9269
Salstrom JS, Pratt D (1971) Role of coliphage M 13 gene 5 in single-stranded DNA production. J Mol Biol 61: 489–501
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
McPherson, A., Wang, A., Jurnak, F., Molineux, I., Rich, A. (1980). Structure of the Gene 5 DNA Binding Protein from Bacteriophage fd and its DNA Binding Cleft. In: Chapeville, F., Haenni, AL. (eds) Chemical Recognition in Biology. Molecular Biology, Biochemistry and Biophysics, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81503-4_19
Download citation
DOI: https://doi.org/10.1007/978-3-642-81503-4_19
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-81505-8
Online ISBN: 978-3-642-81503-4
eBook Packages: Springer Book Archive