USO1 is one of the essential genes in Saccharomyces cerevisiae whose gene products participate in protein transport from the endoplasmic reticulum to the Golgi apparatus. This product was purified to homogeneity. Electron microscopic study revealed that it has a single or double globular domain with a long tail and that the molecule is a dimer. A peak position of the distribution of rod length was 154.5 nm, in agreement with the secondary structure prediction that it has a long alpha-helix at the carboxyl terminus. Probability of coiled-coil formation was also predicted from the primary structure of the product, which asserts that it has a long alpha-helical coiled-coil at the carboxyl-terminal region with some interruptions. Certainly, the electron microscopic image of this molecule had some hinges within the rod region. The distance was measured between the globular domain and the hinges. Two peaks of the distribution of the hinge position exist at 23.1 and 85.5 nm from the globular domain. This is consistent with the predicted positions of interruption. These results give new experimental evidence that Uso1 protein is a dimer and has an alpha-helical coiled-coil tail with two globular heads.
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http://dx.doi.org/10.1006/jsbi.1996.0053 | DOI Listing |
J Colloid Interface Sci
January 2025
Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, 153-8904, Tokyo, Japan; Institute of Industrial Science, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, 153-8505, Tokyo, Japan. Electronic address:
Phase separation, a fundamental phenomenon in both natural and industrial settings, involves the coarsening of domains over time t to reduce interfacial energy. While well-understood for simple viscous liquid mixtures, the physical laws governing coarsening dynamics in complex fluids, such as colloidal suspensions, remain unclear. Here, we investigate colloidal phase separation through particle-based simulations with and without hydrodynamic interactions (HIs).
View Article and Find Full Text PDFBiomater Sci
January 2025
Department of Biological Sciences and Engineering Indian Institute of Technology, Palaj, Gandhinagar 382355, India.
The application of nanotechnology in medical biology has seen a significant rise in recent years because of the introduction of novel tools that include supramolecular systems, complexes, and composites. Dendrimers are one of the remarkable examples of such tools. These spherical, regularly branching structures with enhanced cell compatibility and bioavailability have shown to be an excellent option for gene or drug administration.
View Article and Find Full Text PDFJ Biol Chem
January 2025
Departamento de Bioquímica, IQ, Universidade de São Paulo, 05508-000, São Paulo, Brazil.
The Min system is a key spatial regulator of cell division in rod-shaped bacteria and the first FtsZ negative modulator to be recognized. Nevertheless, despite extensive genetic and in vitro studies, the molecular mechanism used by MinC to inhibit Z-ring formation remains incompletely understood. The crystallization of FtsZ in complex with other negative regulators such as SulA and MciZ has provided important structural information to corroborate in vitro experiments and establish the mechanism of Z-ring antagonism by these modulators.
View Article and Find Full Text PDFJ Chem Phys
January 2025
CNRS, Laboratoire PHENIX (Physicochimie des Electrolytes et Nanosystèmes Interfaciaux), Sorbonne Université, 4 Place Jussieu, 75005 Paris, France.
By means of a minimal physical model, we investigate the interplay of two phase transitions at play in chromatin organization: (1) liquid-liquid phase separation within the fluid solvating chromatin, resulting in the formation of biocondensates; and (2) the coil-globule crossover of the chromatin fiber, which drives the condensation or extension of the chain. In our model, a species representing a domain of chromatin is embedded in a binary fluid. This fluid phase separates to form a droplet rich in a macromolecule (B).
View Article and Find Full Text PDFMol Ther
December 2024
Center for Inflammation, Immunity & Infection, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303, USA. Electronic address:
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