1,657 research outputs found
Active water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay.
We detect internal water molecules in a membrane-embedded receptor-transducer complex and demonstrate water structure changes during formation of the signaling state. Time-resolved FTIR spectroscopy reveals stimulus-induced repositioning of one or more structurally active water molecules to a significantly more hydrophobic environment in the signaling state of the sensory rhodopsin II (SRII)-transducer (HtrII) complex. These waters, distinct from bound water molecules within the SRII receptor, appear to be in the middle of the transmembrane interface region near the Tyr199(SRII)-Asn74(HtrII) hydrogen bond. We conclude that water potentially plays an important role in the SRII --\u3e HtrII signal transfer mechanism in the membrane\u27s hydrophobic core
Synthesis of a gene for sensory rhodopsin I and its functional expression in Halobacterium halobium.
Fine-Structure Map of the Histidine Transport Genes in \u3cem\u3eSalmonella typhimurium\u3c/em\u3e
Afine-structure genetic map of the histidine transport region of the Salmonella typhimurium chromosome was constructed. Twenty-five deletion mutants were isolated and used for dividing the hisJ and hisP genes into 8 and 13 regions respectively. A total of 308 mutations, spontaneous and mutagen induced, have been placed in these regions by deletion mapping. The histidine transport operon is presumed to be constituted of genes dhuA, hisJ, and hisP, and the regulation of the hosP and hisJ genes by dhuA is discussed. The orientation of this operon relative to purF has been established by three-point crosses as being: purF duhA hisJ hisP
Internal Motility in Stiffening Actin-Myosin Networks
We present a study on filamentous actin solutions containing heavy meromyosin
subfragments of myosin II motor molecules. We focus on the viscoelastic phase
behavior and internal dynamics of such networks during ATP depletion. Upon
simultaneously using micro-rheology and fluorescence microscopy as
complementary experimental tools, we find a sol-gel transition accompanied by a
sudden onset of directed filament motion. We interpret the sol-gel transition
in terms of myosin II enzymology, and suggest a "zipping" mechanism to explain
the filament motion in the vicinity of the sol-gel transition.Comment: 4 pages, 3 figure
Attractant and Repellent Signaling Conformers of Sensory RhodopsinâTransducer Complexesâ
ABSTRACT: Attractant and repellent signaling conformers of the dual-signaling phototaxis receptor sensory rhodopsin I and its transducer subunit (SRI-HtrI) have recently been distinguished experimentally by the opposite connection of their retinylidene protonated Schiff bases to the outwardly located periplasmic side and inwardly located cytoplasmic side. Here we show that the pKa of the outwardly located Asp76 counterion in the outwardly connected conformer is lowered by âŒ1.5 units from that of the inwardly connected conformer. The pK a difference enables quantitative determination of the relative amounts of the two conformers in wild-type cells and behavioral mutants prior to photoexcitation, comparison of their absorption spectra, and determination of their relative signaling efficiency. We have shown that the onephoton excitation of the SRI-HtrI attractant conformer causes a Schiff base connectivity switch from inwardly connected to outwardly connected states in the attractant signaling photoreaction. Conversely, a second near-UV photon drives the complex back to the inwardly connected conformer in the repellent signaling photoreaction. The results suggest a model of the color-discriminating dual-signaling mechanism in which phototaxis responses (his-kinase modulation) result from the photointerconversion of the two oppositely connected SRI-HtrI conformers by one-photon and two-photon activation. Furthermore, we find that the related repellent phototaxis SRII-HtrII receptor complex has an outwardly connecte
Structural Transition of Actin Filament in a Cell-Sized Water Droplet with a Phospholipid Membrane
Actin filament, F-actin, is a semiflexible polymer with a negative charge,
and is one of the main constituents on cell membranes. To clarify the effect of
cross-talk between a phospholipid membrane and actin filaments in cells, we
conducted microscopic observations on the structural changes in actin filaments
in a cell-sized (several tens of micrometers in diameter) water droplet coated
with a phospholipid membrane such as phosphatidylserine (PS; negatively-charged
head group) or phosphatidylethanolamine (PE; neutral head group) as a simple
model of a living cell membrane. With PS, actin filaments are distributed
uniformly in the water phase without adsorption onto the membrane surface
between 2 and 6 mM Mg2+, while between 6 and 12 mM Mg2+, actin filaments are
adsorbed onto the inner membrane surface. With PE, actin filaments are
uniformly adsorbed onto the inner membrane surface between 2 and 12 mM Mg2+.
With both PS and PE membranes, at Mg2+ concentrations higher than 12 mM, thick
bundles are formed in the bulk water droplet accompanied by the dissolution of
actin filaments from the membrane surface. The attraction between actin
filaments and membrane is attributable to an increase in the translational
entropy of counterions accompanied by the adsorption of actin filaments onto
the membrane surface. These results suggest that a microscopic water droplet
coated with phospholipid can serve as an easy-to-handle model of cell
membranes
Fluctuating-friction molecular motors
We show that the correlated stochastic fluctuation of the friction
coefficient can give rise to long-range directional motion of a particle
undergoing Brownian random walk in a constant periodic energy potential
landscape. The occurrence of this motion requires the presence of two
additional independent bodies interacting with the particle via friction and
via the energy potential, respectively, which can move relative to each other.
Such three-body system generalizes the classical Brownian ratchet mechanism,
which requires only two interacting bodies. In particular, we describe a simple
two-level model of fluctuating-friction molecular motor that can be solved
analytically. In our previous work [M.K., L.M and D.P. 2000 J. Nonlinear Opt.
Phys. Mater. vol. 9, 157] this model has been first applied to understanding
the fundamental mechanism of the photoinduced reorientation of dye-doped liquid
crystals. Applications of the same idea to other fields such as molecular
biology and nanotechnology can however be envisioned. As an example, in this
paper we work out a model of the actomyosin system based on the
fluctuating-friction mechanism.Comment: to be published in J. Physics Condensed Matter
(http://www.iop.org/Journals/JPhysCM
Polymer Induced Bundling of F-actin and the Depletion Force
The inert polymer polyethylene glycol (PEG) induces a "bundling" phenomenon
in F-actin solutions when its concentration exceeds a critical onset value C_o.
Over a limited range of PEG molecular weight and ionic strength, C_o can be
expressed as a function of these two variables. The process is reversible, but
hysteresis is also observed in the dissolution of the bundles, with ionic
strength having a large influence. Additional actin filaments are able to join
previously formed bundles. Little, if any, polymer is associated with the
bundle structure.
Continuum estimates of the Asakura-Oosawa depletion force, Coulomb repulsion,
and van der Waals potential are combined for a partial explanation of the
bundling effect and hysteresis. Conjectures are presented concerning the
apparent limit in bundle size
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