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We report on the photo-induced precession of the ferromagnetically coupled Mn spins in (Ga,Mn)As, which is observed even with no external magnetic field applied. We concentrate on various experimental aspects of the time-resolved magneto-optical Kerr effect (TR-MOKE) technique that can be used to clarify the origin of the detected signals. We show that the measured data typically consist of several different contributions, among which only the oscillatory signal is directly connected with the ferromagnetic order in the sample. Index Terms--Dynamic response, magnetic semiconductors, magnetooptic Kerr effect, optical spectroscopy.

The genes encoding the DNA methyltransferases M.NmeDI and M.NmeAI from Neisseria meningitidis associated with the genes encoding putative Vsr endonucleases were overexpressed in Escherichia coli. The enzymes were purified to apparent homogeneity on Ni-NTA agarose columns, yielding proteins of 494 [+ or -] 1 kDa and 39-6 [+ or -] 1 kDa, respectively, under denaturing conditions. M.NmeDI recognizes the degenerate sequence 5'-RCCGGB-3'. It methylates the first 5' cytosine residue on both strands within the core sequence CCGG. The enzyme shows higher affinity with the hemimethylated degenerate sequence than with the unmethylated degenerate sequence. Comparison of the amino acid sequence of the target-recognizing domain of M.NmeDI with the closest neighbours recognizing the sequence 5'-RCCGGY-3' showed the presence of the homologous domain and an additional domain that may be responsible for recognizing the degenerate sequence. M.NmeAI recognizes the sequence 5'-CCGG-3' and methylates the second 5' cytosine residue on both DNA strands. In Neisseria gonorrhoeae strain FA1090 the homologues of these ORFs are truncated due to a variety of mutations.

We report on all-optical detection of magnetization dynamics in the ferromagnetic semiconductor (Ga,Mn)As in the presence of spin-wave resonances (SWRs) using a time-resolved magneto-optical (TRMO) technique. In our previous experiments, we demonstrated the possibility to reconstruct the magnetization dynamics directly from the TRMO signals. In this paper, we present a detailed time-domain analysis of the TRMO traces obtained using this method to determine the exact influence of the higher SWR modes on the laser-induced magnetization dynamics. We focus on the effect of the SWR on the evolution of the spatially averaged magnetization. [ABSTRACT FROM AUTHOR]

This paper assesses the instrumental resolution of a mechanical extensometer in light of its recent automatisation. The instrument takes advantage of the moire phenomenon of optical interference to measure angular rotation in two perpendicular planes and displacement in three dimensions. Our assessment systematically defines an analytical solution for the complete interpretation of a generic moire pattern and a set of mathematical approximations for the moire patterns used to measure rotation and displacement. The ultimate sensitivity of the automated instrument is determined on the basis of a generic least square differences fitting procedure while the instrumental resolution is defined on the basis of realistic, rather than optimal, scenarios: the resolution of the rotation measurements are in the order of 8.7 ∗ 10 −5 rad while the resolution of the displacement measurements are better than 5 μm. This assessment represents the first step towards a global numerical repository for processed data recorded by the automated extensometers. [ABSTRACT FROM AUTHOR]

Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro and is an important factor in the cellular response to diverse biotic and abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However the molecular mechanism of AtNUDT7 function remains elusive. To gain a better understanding of this hydrolase cellular role, proteins interacting with AtNUDT7 were identified. Using AtNUDT7 as a bait in an in vitro binding assay of proteins derived from cultured Arabidopsis cell extracts we identified the regulatory protein RACK1A as an AtNUDT7-interactor. RACK1A-AtNUDT7 interaction was confirmed in a yeast two-hybrid assay and in a pull-down assay and in Bimolecular Fluorescence Complementation (BiFC) analysis of the proteins transiently expressed in Arabidopsis protoplasts. However, no influence of RACK1A on AtNUDT7 hydrolase catalytic activity was observed. In vitro interaction between RACK1A and the AGG1 and AGG2 gamma subunits of the signal transducing heterotrimeric G protein was also detected and confirmed in BiFC assays. Moreover, association between AtNUDT7 and both AGG1 and AGG2 subunits was observed in Arabidopsis protoplasts, although binding of these proteins could not be detected in vitro. Based on the observed interactions we conclude that the AtNUDT7 Nudix hydrolase forms complexes in vitro and in vivo with regulatory proteins involved in signal transduction. Moreover, we provide the initial evidence that both signal transducing gamma subunits bind the regulatory RACK1A protein.

Arabidopsis thaliana AtNUDT7, a homodimeric Nudix hydrolase active on ADP-ribose and NADH, exerts negative control on the major signaling complex involved in plant defense activation and programmed cell death. The structural and functional consequences of altering several amino-acid residues of the AtNUDT7 protein have been examined by site-directed mutagenesis, far-UV circular dichroism (CD), attenuated total reflection-Fourier transform infrared (ATR-FTIR) and photon correlation (PCS) spectroscopy, biochemical analysis and protein-protein interaction studies. Alanine substitutions of F73 and V168 disallowed dimer formation. Both the F73A- and V168A-mutated proteins displayed no observable enzymatic activity. Alanine substitution of the V69 residue did not significantly alter the enzyme activity and had no influence on dimer arrangement. The non-conserved V26 residue, used as a negative control, did not contribute to the enzyme quaternary structure or activity. Detailed biophysical characterization of the wild-type and mutant proteins indicates that the mutations do not considerably alter the secondary structure of the enzyme but they affect dimer assembly. In addition, mutating residues V69, F73 and V168 disrupted the binding of AtNUDT7 to the regulatory 14.3.3 protein. These are the first studies of the structure-function relationship of AtNUDT7, a Nudix hydrolase of important regulatory function.