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Stanley Brown

Publications and source records attributed to Stanley Brown.

2 recordsLinked to original sources

Stability puzzles in phage lambda.

In the absence of RecA-mediated cleavage of the repressor, the lambda prophage is exceptionally stable. We develop a stochastic model that predicts the stability of such epigenetic states from affinities of the molecular components. We find that the stability, in particular, depends on the maximum possible cI protein production, and on the number of translated cro proteins per transcribed mRNA. We apply the model to the behavior of recently published mutants of O(R) and find, in particular, that a mutant that overexpress cro behaves in a different way than what was predicted, thus suggesting that the current view of the O(R) switch is incomplete. The approach described here should be generally applicable to the stability of expressed states.

Journal Article↗

The motion of a single molecule, the lambda-receptor, in the bacterial outer membrane.

Using optical tweezers and single particle tracking, we have revealed the motion of a single protein, the lambda-receptor, in the outer membrane of living Escherichia coli bacteria. We genetically modified the lambda-receptor placing a biotin on an extracellular site of the receptor in vivo. The efficiency of this in vivo biotinylation is very low, thus enabling the attachment of a streptavidin-coated bead binding specifically to a single biotinylated lambda-receptor. The bead was used as a handle for the optical tweezers and as a marker for the single particle tracking routine. We propose a model that allows extraction of the motion of the protein from measurements of the mobility of the bead-molecule complex; these results are equally applicable to analyze bead-protein complexes in other membrane systems. Within a domain of radius approximately 25 nm, the receptor diffuses with a diffusion constant of (1.5 +/- 1.0) x 10(-9) cm(2)/s and sits in a harmonic potential as if it were tethered by an elastic spring of spring constant of ~1.0 x 10(-2) pN/nm to the bacterial membrane. The purpose of the protein motion might be to facilitate transport of maltodextrins through the outer bacterial membrane.

Bacterial Outer Membrane Proteins↗