Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.

The activation of ubiquitin and related protein modifiers is catalysed by members of the E1 enzyme family that use ATP for the covalent self-attachment of the modifiers to a conserved cysteine. The Escherichia coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis, an evolutionarily conserved pathway. The MoeB- and E1-catalysed reactions are mechanistically similar, and despite a lack of sequence similarity, MoaD and ubiquitin display the same fold including a conserved carboxy-terminal Gly-Gly motif. Similar to the E1 enzymes, MoeB activates the C terminus of MoaD to form an acyl-adenylate. Subsequently, a sulphurtransferase converts the MoaD acyl-adenylate to a thiocarboxylate that acts as the sulphur donor during Moco biosynthesis. These findings suggest that ubiquitin and E1 are derived from two ancestral genes closely related to moaD and moeB. Here we present the crystal structures of the MoeB-MoaD complex in its apo, ATP-bound, and MoaD-adenylate forms, and highlight the functional similarities between the MoeB- and E1-substrate complexes. These structures provide a molecular framework for understanding the activation of ubiquitin, Rub, SUMO and the sulphur incorporation step during Moco and thiamine biosynthesis.     

SB-restricted presentation of influenza and herpes simplex virus antigens to human T-lymphocyte clones

The HLA-D region of the human major histocompatibility complex (MHC) has been shown to be homologous to the murine I region in terms of both structure and function. Both regions encode class II MHC molecules which restrict T-lymphocyte interactions with antigen-presenting cells. We have recently described the MHC restriction and antigen specificities of human T-lymphocyte clones directed at strain A influenza virus. The majority of T-lymphocyte clones recognized antigen in the context of cell surface interaction products encoded by HLA-D/DR genes. However, a few clones recognized antigen presented by cells histoincompatible for D/DR antigens. We report here that some of these clones recognized viral antigens in association with antigens encoded by genes identical with or closely linked to the recently described secondary B-cell (SB) locus of the MHC. This is the first report that SB-restricted antigen recognition may form an integral part of normal, human immune responses.     

Origin of the eukaryotic nucleus determined by rate-invariant analysis of rRNA sequences

The origin of the eukaryotic nucleus is difficult to reconstruct. Eukaryotic organelles (chloroplast, mitochondrion) are eubacterial endosymbionts, but the source of nuclear genes has been obscured by multiple nucleotide substitutions. Using evolutionary parsimony, a newly developed rate-invariant treeing algorithm, the eukaryotic ribosomal rRNA genes are shown to have evolved from the eocytes, a group of extremely thermophilic, sulphur-metabolizing, anucleate cells. The deepest bifurcation yet found separates the reconstructed tree into two taxonomic divisions. These are a proto-eukaryotic group (karyotes) and an essentially bacterial one (parkaryotes). Within the precision of the rooting procedure, the tree is not consistent with either the prokaryotic-eukaryotic or the archaebacterial-eubacterial-eukaryotic groupings. It implies that the last common ancestor of extant life, and the early ancestors of eukaryotes, probably lacked nuclei, metabolized sulphur and lived at near-boiling temperatures.     

Changes in the histochemical nature of neurosecretory materials during axonal transport in the CrabParagrapsus gaimardii

Résumé Dans le système neurosécréteur du pédoncule oculaire et les organes péricardiques du crabeParagrapsus gaimardii, la direction du processus de modification du produit de neurosécrétion durant le cheminement axonal semble Être de sens opposé à celle qu'on observe chez les insectes et les grenouilles.     

Antiferromagnetic order induced by an applied magnetic field in a high-temperature superconductor.

One view of the high-transition-temperature (high-Tc) copper oxide superconductors is that they are conventional superconductors where the pairing occurs between weakly interacting quasiparticles (corresponding to the electrons in ordinary metals), although the theory has to be pushed to its limit. An alternative view is that the electrons organize into collective textures (for example, charge and spin stripes) which cannot be 'mapped' onto the electrons in ordinary metals. Understanding the properties of the material would then need quantum field theories of objects such as textures and strings, rather than point-like electrons. In an external magnetic field, magnetic flux penetrates type II superconductors via vortices, each carrying one flux quantum. The vortices form lattices of resistive material embedded in the non-resistive superconductor, and can reveal the nature of the ground state-for example, a conventional metal or an ordered, striped phase-which would have appeared had superconductivity not intervened, and which provides the best starting point for a pairing theory. Here we report that for one high-Tc superconductor, the applied field that imposes the vortex lattice also induces 'striped' antiferromagnetic order. Ordinary quasiparticle models can account for neither the strength of the order nor the nearly field-independent antiferromagnetic transition temperature observed in our measurements.