284 research outputs found

    The Internet and the Hobbs Act: What’s the Connection?

    Get PDF
    The Hobbs Act provides a federal alternative to traditional state robbery charges by criminalizing any robbery that affects interstate commerce. Courts have interpreted the Hobbs Act’s commerce element broadly, by requiring the government to demonstrate that a robbery had a de minimis effect on interstate commerce. With this standard, robberies of businesses generally satisfy the statute’s commerce element, but robberies of individuals often do not. This difference between a state and a federal robbery charge is significant, because the Hobbs Act generally carries substantially harsher penal sentences. This Note examines when the use of the internet in the robbery of an individual should satisfy the Hobbs Act’s commerce element. With the internet’s prominent role in society, the answer to this issue could impact whether countless robberies can be charged as federal crimes. This Note, therefore, contends that courts should adopt a functional test to determine, on a case-by-case basis, whether internet use in a robbery satisfies the Hobbs Act’s commerce element. Adoption of this test would align with Commerce Clause case law and Hobbs Act case law. Furthermore, it would promote federalism and safeguard the traditional role of federal courts

    Role of the N- and C-terminal extensions on the activity of mammalian mitochondrial translational initiation factor 3

    Get PDF
    Mammalian mitochondrial translational initiation factor 3 (IF3(mt)) promotes initiation complex formation on mitochondrial 55S ribosomes in the presence of IF2(mt), fMet-tRNA and poly(A,U,G). The mature form of IF3(mt) is predicted to be 247 residues. Alignment of IF3(mt) with bacterial IF3 indicates that it has a central region with 20–30% identity to the bacterial factors. Both the N- and C-termini of IF3(mt) have extensions of ∼30 residues compared with bacterial IF3. To examine the role of the extensions on IF3(mt), deletion constructs were prepared in which the N-terminal extension, the C-terminal extension or both extensions were deleted. These truncated derivatives were slightly more active in promoting initiation complex formation than the mature form of IF3(mt). Mitochondrial 28S subunits have the ability to bind fMet-tRNA in the absence of mRNA. IF3(mt) promotes the dissociation of the fMet-tRNA bound in the absence of mRNA. This activity of IF3(mt) requires the C-terminal extension of this factor. Mitochondrial 28S subunits also bind mRNA independently of fMet-tRNA or added initiation factors. IF3(mt) has no effect on the formation of these complexes and cannot dissociate them once formed. These observations have lead to a new model for the function of IF3(mt) in mitochondrial translational initiation

    Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange

    Get PDF
    AbstractThe guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg2+ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2–3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Tsmt were 5–10-fold less active in stimulating the activity of EF-Tumt. The double mutation completely abolished the activity of EF-Tsmt

    Interaction of Mammalian Mitochondrial Ribosomes with the Inner Membrane

    Get PDF
    All of the products of mitochondrial protein biosynthesis in animals are hydrophobic proteins that are localized in the inner membrane. Hence, it is possible that the synthesis of these proteins could occur on ribosomes associated with the inner membrane. To examine this possibility, inner membrane and matrix fractions of bovine mitochondria were examined for the presence of ribosomes using probes for the rRNAs. Between 40 and 50% of the ribosomes were found to fractionate with the inner membrane. About half of the ribosomes associated with the inner membrane could be released by high salt treatment, indicating that they interact with the membrane largely through electrostatic forces. No release of the ribosome was observed upon treatment with puromycin, suggesting that the association observed is not due to insertion of a nascent polypeptide chain into the membrane. A fraction of the ribosomes remained with residual portions of the membranes that cannot be solubilized in the presence of Triton X-100. These ribosomes may be associated with large oligomeric complexes in the membrane
    • …
    corecore