New complexes of formulae [Cu(HL(2))(H(2)O)(NO(3))](NO(3)) (1), [{Cu(L(1))(tfa)}(2)] (2), [{Cu(L(1))}(2)(pz)](ClO(4))(2) (3) and {[{Cu(L(1))}(2)(dca)](ClO(4))}(n) (4), where HL(1)=pyridine-2-carbaldehyde thiosemicarbazone, HL(2)=pyridine-2-carbaldehyde 4N-methylthiosemicarbazone, Htfa=trifluoroacetic acid (CF(3)COOH), pz=pyrazine (C(4)H(4)N(2)) and dca=dicyanamide [N(CN)(2)](-), have been synthesized and characterized. The crystal structures of these compounds are built up of monomers (1), dinuclear entities with the metal centers bridged through the non-thiosemicarbazone coligand (2 and 3) and 1D chains of dimers (4). In all the cases, square-pyramidal copper(II) ions are present, except for the square-planar ones in 3. Magnetic measurements show antiferromagnetic couplings in 2, 3 and 4. The susceptibility data were fitted by the Bleaney-Bowers' equation for copper(II) dimers derived from H=-2JS(1)S(2) being the obtained J/k values -4.8, -4.3 and -5.1K for compounds 2-4, respectively. The magnetic susceptibility of the already known [{Cu(HL(1))(tfa)}(2)](tfa)(2) compound has been also measured for the first time. The J/k value is -0.3K, lower than that in 2. The nuclease activity of 3 and 4 has been analyzed.
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http://dx.doi.org/10.1016/j.jinorgbio.2008.06.015 | DOI Listing |
J Biol Chem
December 2024
Division of Biological Sciences, Indian Institute of Science, Bangalore 560 012. Electronic address:
Paralogues of the bifunctional nuclease, Ribonuclease J (RNase J) demonstrate varied catalytic efficiencies despite extensive sequence and structural similarity. Of the two S. aureus RNase J paralogues, RNase J1 is substantially more active than RNase J2.
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December 2024
Department of Biochemistry, University of Zurich, Zurich, Switzerland. Electronic address:
The detection of molecular patterns associated with invading pathogens is a hallmark of innate immune systems. Prokaryotes deploy sophisticated host defense mechanisms in innate anti-phage immunity. Shedu is a single-component defense system comprising a putative nuclease SduA.
View Article and Find Full Text PDFMol Cell
December 2024
Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA, USA; Department of Molecular Biology, University of California, San Diego, La Jolla, CA, USA. Electronic address:
Prokaryotes possess diverse anti-bacteriophage immune systems, including the single-protein Shedu nuclease. Here, we reveal the structural basis for activation of Bacillus cereus Shedu. Two cryoelectron microscopy structures of Shedu show that it switches between inactive and active states through conformational changes affecting active-site architecture, which are controlled by the protein's N-terminal domain (NTD).
View Article and Find Full Text PDFNat Commun
December 2024
Laboratory of Retrovirology, The Rockefeller University, New York, NY, 10065, USA.
ZAP is an antiviral protein that binds to and depletes viral RNA, which is often distinguished from vertebrate host RNA by its elevated CpG content. Two ZAP cofactors, TRIM25 and KHNYN, have activities that are poorly understood. Here, we show that functional interactions between ZAP, TRIM25 and KHNYN involve multiple domains of each protein, and that the ability of TRIM25 to multimerize via its RING domain augments ZAP activity and specificity.
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December 2024
Beijing Frontier Research Center for Biological Structure, State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Exceptionally diverse type V CRISPR-Cas systems provide numerous RNA-guided nucleases as powerful tools for DNA manipulation. Two known Cas12e nucleases, DpbCas12e and PlmCas12e, are both effective in genome editing. However, many differences exist in their in vitro dsDNA cleavage activities, reflecting the diversity in Cas12e's enzymatic properties.
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