Protein-hydrocarbon interactions. Interactions of various proteins with pure decane.
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ABSTRACT:
SUBMITTER: Cecil R
PROVIDER: S-EPMC1178839 | biostudies-other | 1970 Mar
REPOSITORIES: biostudies-other
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Project description:1. Solutions of proteins were subjected to gentle agitation in the presence of small quantities of decane containing different alcohols. 2. Some of the protein was lost from solution and adsorbed on the surface of the emulsion formed; at the same time some decane was bound to the protein remaining in solution. 3. Comparison of these results with those obtained with pure decane suggests that a mixed film of protein+alcohol is formed on the surface of the emulsion. 4. If the concentration of alcohol in decane is increased the amount of protein adsorbed on the emulsion is decreased. This phenomenon was used to compare the effect of different alcohols in disrupting the hydrophobic interactions between proteins and hydrocarbons.
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Project description:Chromatin remodelers regulate genes by organizing nucleosomes around promoters, but their individual contributions are obfuscated by the complex in vivo milieu of factor redundancy and indirect effects. Genome-wide reconstitution of promoter nucleosome organization with purified proteins resolves this problem and is therefore a critical goal. Here, we reconstitute four stages of nucleosome architecture using purified components: yeast genomic DNA, histones, sequence-specific Abf1/Reb1, and remodelers RSC, ISW2, INO80, and ISW1a. We identify direct, specific, and sufficient contributions that in vivo observations validate. First, RSC clears promoters by translating poly(dA:dT) into directional nucleosome removal. Second, partial redundancy is recapitulated where INO80 alone, or ISW2 at Abf1/Reb1sites, positions +1 nucleosomes. Third, INO80 and ISW2 each align downstream nucleosomal arrays. Fourth, ISW1a tightens the spacing to canonical repeat lengths. Such a minimal set of rules and proteins establishes core mechanisms by which promoter chromatin architecture arises through a blend of redundancy and specialization.
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