Hydrodynamic studies of a DNA-protein complex: Elongation of single stranded nucleic acids upon complexation with the gene 32 protein of phage T4 deduced from electric field-induced birefringence experiments

Short DNA and RNA fragments complexed with the helix destabilizing protein of bacteriophage T4, GP32, have been studied in solution by electric birefringence and circular dichroism. The birefringence of the complexes is positive and the magnitude indicates that the DNA and RNA fragments become linea...

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Bibliographic Details
Published in:FEBS letters 1985-01, Vol.179 (2), p.221-224
Main Authors: Scheerhagen, M.A., van Amerongen, H., van Grondelle, R., Blok, Joh
Format: Article
Language:English
Subjects:
Bacteriophage T4
Biological and medical sciences
Birefringence
Chemical Phenomena
Chemistry, Physical
Circular Dichroism
DNA - metabolism
DNA-protein complex
Electric birefringence Axial increment determination
Fundamental and applied biological sciences. Psychology
Helix destabilizing protein
Interactions. Associations
Intermolecular phenomena
Molecular biophysics
phage T4
RNA, Bacterial - metabolism
RNA, Fungal - metabolism
Solutions
Viral Proteins - metabolism
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Summary:Short DNA and RNA fragments complexed with the helix destabilizing protein of bacteriophage T4, GP32, have been studied in solution by electric birefringence and circular dichroism. The birefringence of the complexes is positive and the magnitude indicates that the DNA and RNA fragments become linear and rigid upon protein binding. The field free decay is biphasic. On the basis of a rigid rod approximation the slow relaxation time leads to a base-base distance along the helix axis in the complex from 4.3 to 5.6 Å, an elongation of at least 50% compared to single-stranded DNA.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80522-6