Linked Life Data

19084023

Source:http://linkedlifedata.com/resource/pubmed/id/19084023

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2009-2-2
pubmed:abstractText
Protein p6 from Bacillus subtilis phage phi29 binds double-stranded DNA, forming a large nucleoprotein complex all along the viral genome, and has been proposed to be an architectural protein with a global role in genome organization. Here, we have characterized quantitatively the DNA binding properties of protein p6 by means of sedimentation velocity and sedimentation equilibrium experiments permitting determination of the strength and stoichiometry of complex formation. The composition dependence of protein binding to DNA is quantitatively consistent with a model in which the protein undergoes a reversible monomer-dimer self-association, and the dimeric species binds noncooperatively to the DNA. We also have found that when the anisotropic bendability periodicity of the nucleotide sequence preferred by p6 is modified, nucleocomplex formation is impaired. In addition, suppression of complex formation at high ionic strength is reversed by the addition of high concentrations of an inert polymer, mimicking the crowded intracellular environment. The results obtained in this work illustrate how macromolecular crowding could act as a metabolic buffer that can significantly extend the range of intracellular conditions under which a specific reaction may occur.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1616-29
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Analytical ultracentrifugation studies of phage phi29 protein p6 binding to DNA.
pubmed:affiliation
Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't