137 research outputs found
Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration
Many species of the bacterial Shewanella genus are notable for their ability to respire in anoxic environments utilizing insoluble minerals of Fe(III) and Mn(IV) as extracellular electron acceptors. In Shewanella oneidensis, the process is dependent on the decahaem electron-transport proteins that lie at the extracellular face of the outer membrane where they can contact the insoluble mineral substrates. These extracellular proteins are charged with electrons provided by an inter-membrane electron-transfer pathway that links the extracellular face of the outer membrane with the inner cytoplasmic membrane and thereby intracellular electron sources. In the present paper, we consider the common structural features of two of these outer-membrane decahaem cytochromes, MtrC and MtrF, and bring this together with biochemical, spectroscopic and voltammetric data to identify common and distinct properties of these prototypical members of different clades of the outer-membrane decahaem cytochrome superfamily
First Steps Towards Radical Parametrization of Algebraic Surfaces
We introduce the notion of radical parametrization of a surface, and we
provide algorithms to compute such type of parametrizations for families of
surfaces, like: Fermat surfaces, surfaces with a high multiplicity (at least
the degree minus 4) singularity, all irreducible surfaces of degree at most 5,
all irreducible singular surfaces of degree 6, and surfaces containing a pencil
of low-genus curves. In addition, we prove that radical parametrizations are
preserved under certain type of geometric constructions that include offset and
conchoids.Comment: 31 pages, 7 color figures. v2: added another case of genus
Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
We examined the role of regulatory myosin light chain (MLC) phosphorylation of myosin II in cell migration of fibroblasts. Myosin light chain kinase (MLCK) inhibition blocked MLC phosphorylation at the cell periphery, but not in the center. MLCK-inhibited cells did not assemble zyxin-containing adhesions at the periphery, but maintained focal adhesions in the center. They generated membrane protrusions all around the cell, turned more frequently, and migrated less effectively. In contrast, Rho-associated kinase (ROCK) inhibition blocked MLC phosphorylation in the center, but not at the periphery. ROCK-inhibited cells assembled zyxin-containing adhesions at the periphery, but not focal adhesions in the center. They moved faster and more straight. On the other hand, inhibition of myosin phosphatase increased MLC phosphorylation and blocked peripheral membrane ruffling, as well as turnover of focal adhesions and cell migration. Our results suggest that myosin II activated by MLCK at the cell periphery controls membrane ruffling, and that the spatial regulation of MLC phosphorylation plays critical roles in controlling cell migration of fibroblasts
Characterization of an electron conduit between bacteria and the extracellular environment
A number of species of Gram-negative bacteria can use insoluble minerals of Fe(III) and Mn(IV) as extracellular respiratory electron acceptors. In some species of Shewanella, deca-heme electron transfer proteins lie at the extracellular face of the outer membrane (OM), where they can interact with insoluble substrates. To reduce extracellular substrates, these redox proteins must be charged by the inner membrane/periplasmic electron transfer system. Here, we present a spectro-potentiometric characterization of a trans-OM icosa-heme complex, MtrCAB, and demonstrate its capacity to move electrons across a lipid bilayer after incorporation into proteoliposomes. We also show that a stable MtrAB subcomplex can assemble in the absence of MtrC; an MtrBC subcomplex is not assembled in the absence of MtrA; and MtrA is only associated to the membrane in cells when MtrB is present. We propose a model for the modular organization of the MtrCAB complex in which MtrC is an extracellular element that mediates electron transfer to extracellular substrates and MtrB is a trans-OM spanning Ăź-barrel protein that serves as a sheath, within which MtrA and MtrC exchange electrons. We have identified the MtrAB module in a range of bacterial phyla, suggesting that it is widely used in electron exchange with the extracellular environment
Molecular structure and free energy landscape for electron transport in the decahaem cytochrome MtrF
Semisimplicity of the quantum cohomology for smooth Fano toric varieties associated with facet symmetric polytopes
The degree zero part of the quantum cohomology algebra of a smooth Fano toric
symplectic manifold is determined by the superpotential function, W, of its
moment polytope. In particular, this algebra is semisimple, i.e. splits as a
product of fields, if and only if all the critical points of W are
non-degenerate. In this paper we prove that this non-degeneracy holds for all
smooth Fano toric varieties with facet-symmetric duals to moment polytopes.Comment: 16 pages; corrected version, published in Electron. Res. Announc.
Math. Sc
Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides
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