Literature DB >> 7046792

Neutron scattering data on reconstituted complexes of fd deoxyribonucleic acid and gene 5 protein show that the deoxyribonucleic acid is near the center.

D M Gray, C W Gray, R D Carlson.   

Abstract

We have performed low-angle neutron scattering studies on reconstituted complexes of fd DNA and the gene 5 protein that is produced during infection of Escherichia coli by filamentous fd phage. Essentially identical helical complexes have been made with normal protonated DNA or DNA in which at least 87% of the nonexchangeable protons are replaced by deuterium. From neutron scattering profiles of both complexes over a range of D2O/H2O solvent mixtures, the DNA deuteration is shown to have a dramatic influence on the measured cross-sectional radius of gyration. Most importantly, data for the complex containing deuterated DNA lead to a more negative slope in a plot of the square of the cross-sectional radius of gyration vs. the inverse of the solute-solvent contrast, compared with the slope of a plot of data for the complex containing protonated DNA. This means that, in a cross-sectional view of the complex, the DNA is near the center of the structure. By our analysis, the DNA has a cross-sectional radius of gyration of 17.6 +/- 3 A, while the protein has a cross-sectional radius of gyration of about 33.5 A. Therefore, the model for the structure of the helical complex that has been proposed from X-ray diffraction studies on gene 5 protein crystallized with oligodeoxynucleotides [McPherson, A., Jurnak, F., Wang, A., Kolpak, F., Rich, A., Molineux, I., & Fitzgerald, P. (1980) Biophys. J. 32, 155-170] is not valid for the complex in solution. From our neutron diffraction data we have also obtained values for the solvent-excluded volume and mass per unit length. The relation of our findings to the solution structure of the complex is discussed.

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Year:  1982        PMID: 7046792     DOI: 10.1021/bi00540a020

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  9 in total

1.  Direct measurement of oligonucleotide binding stoichiometry of gene V protein by mass spectrometry.

Authors:  X Cheng; A C Harms; P N Goudreau; T C Terwilliger; R D Smith
Journal:  Proc Natl Acad Sci U S A       Date:  1996-07-09       Impact factor: 11.205

2.  Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.

Authors:  S Su; Y G Gao; H Zhang; T C Terwilliger; A H Wang
Journal:  Protein Sci       Date:  1997-04       Impact factor: 6.725

Review 3.  Structural studies of proteins by high-flux X-ray and neutron solution scattering.

Authors:  S J Perkins
Journal:  Biochem J       Date:  1988-09-01       Impact factor: 3.857

4.  Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex.

Authors:  Y Guan; H Zhang; A H Wang
Journal:  Protein Sci       Date:  1995-02       Impact factor: 6.725

5.  Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein.

Authors:  M M Skinner; H Zhang; D H Leschnitzer; Y Guan; H Bellamy; R M Sweet; C W Gray; R N Konings; A H Wang; T C Terwilliger
Journal:  Proc Natl Acad Sci U S A       Date:  1994-03-15       Impact factor: 11.205

6.  The binding affinity of Ff gene 5 protein depends on the nearest-neighbor composition of the ssDNA substrate.

Authors:  T C Mou; C W Gray; D M Gray
Journal:  Biophys J       Date:  1999-03       Impact factor: 4.033

7.  Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR.

Authors:  Smadar Kedem; Roni Rene Hassid; Yoav Shamir; Amir Goldbourt
Journal:  Viruses       Date:  2022-06-10       Impact factor: 5.818

8.  Chemical modification of the coat protein in bacteriophage fd and orientation of the virion during assembly and disassembly.

Authors:  J Armstrong; J A Hewitt; R N Perham
Journal:  EMBO J       Date:  1983       Impact factor: 11.598

9.  Solution structure of the single-stranded DNA binding protein of the filamentous Pseudomonas phage Pf3: similarity to other proteins binding to single-stranded nucleic acids.

Authors:  R H Folmer; M Nilges; R N Konings; C W Hilbers
Journal:  EMBO J       Date:  1995-09-01       Impact factor: 11.598

  9 in total

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