Framing the local and the global in the anti-nuclear movement: Law and the politics of place

This article examines the politics of place in relation to legal mobilization by the anti-nuclear movement. It examines two case examples - citizens' weapons inspections and civil disobedience strategies - which have involved the movement drawing upon the law in particular spatial contexts. The article begins by examining a number of factors which have been employed in recent social movement literature to explain strategy choice, including ideology, resources, political and legal opportunity, and framing. It then proceeds to argue that the issues of scale, space, and place play an important role in relation to framing by the movement in the two case examples. Both can be seen to involve scalar reframing, with the movement attempting to resist localizing tendencies and to replace them with a global frame. Both also involve an attempt to reframe the issue of nuclear weapons away from the contested frame of the past (unilateral disarmament) towards the more universal and widely accepted frame of international law.

Cell and nuclear degradation in sweetpotato [Ipomoea batatas (L.) Lam.] root meristems following exposure to salinity

Sodium chloride-induced cell and nuclear degradation in the root meristems of sweetpotato [Ipomoea batatas (L.) Lam.] were determined using fluorescent microscopy and flow cytometry analysis. Two sweetpotato cultivars were grown in liquid Murashige and Skoog medium and subjected to 0 mM and 500 mM NaCl, with or without 15 mM CaCl2, for periods up to 24 h. Changes to the nuclei of root meristematic cells showed a similar pattern of damage to the nuclei using both fluorescent microscopy and flow cytometry analysis. Damage occurring after only a few hours was followed by nuclear degradation at 24 h. Flow cytometry histograms showed a reduction in G1 and G2 nuclei and an increase in degraded nuclei in NaCl-stressed roots. Salinity-induced nuclear degradation was alleviated by the addition of CaCl2.

Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold

The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1 ''-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.

Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3

The nuclear magnetic resonance (NMR) structure of a globular domain of residues 1071 to 1178 within the previously annotated nucleic acid-binding region (NAB) of severe acute respiratory syndrome coronavirus nonstructural protein 3 (nsp3) has been determined, and N- and C-terminally adjoining polypeptide segments of 37 and 25 residues, respectively, have been shown to form flexibly extended linkers to the preceding globular domain and to the following, as yet uncharacterized domain. This extension of the structural coverage of nsp3 was obtained from NMR studies with an nsp3 construct comprising residues 1066 to 1181 [ nsp3(1066-1181)] and the constructs nsp3(1066-1203) and nsp3(1035-1181). A search of the protein structure database indicates that the globular domain of the NAB represents a new fold, with a parallel four-strand beta-sheet holding two alpha-helices of three and four turns that are oriented antiparallel to the beta-strands. Two antiparallel two-strand beta-sheets and two 3(10)-helices are anchored against the surface of this barrel-like molecular core. Chemical shift changes upon the addition of single-stranded RNAs (ssRNAs) identified a group of residues that form a positively charged patch on the protein surface as the binding site responsible for the previously reported affinity for nucleic acids. This binding site is similar to the ssRNA-binding site of the sterile alpha motif domain of the Saccharomyces cerevisiae Vts1p protein, although the two proteins do not share a common globular fold.

Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus

This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.