38,420 research outputs found

    Protein chainmail variants in dsDNA viruses.

    Get PDF
    First discovered in bacteriophage HK97, biological chainmail is a highly stable system formed by concatenated protein rings. Each subunit of the ring contains the HK97-like fold, which is characterized by its submarine-like shape with a 5-stranded β sheet in the axial (A) domain, spine helix in the peripheral (P) domain, and an extended (E) loop. HK97 capsid consists of covalently-linked copies of just one HK97-like fold protein and represents the most effective strategy to form highly stable chainmail needed for dsDNA genome encapsidation. Recently, near-atomic resolution structures enabled by cryo electron microscopy (cryoEM) have revealed a range of other, more complex variants of this strategy for constructing dsDNA viruses. The first strategy, exemplified by P22-like phages, is the attachment of an insertional (I) domain to the core 5-stranded β sheet of the HK97-like fold. The atomic models of the Bordetella phage BPP-1 showcases an alternative topology of the classic HK97 topology of the HK97-like fold, as well as the second strategy for constructing stable capsids, where an auxiliary jellyroll protein dimer serves to cement the non-covalent chainmail formed by capsid protein subunits. The third strategy, found in lambda-like phages, uses auxiliary protein trimers to stabilize the underlying non-covalent chainmail near the 3-fold axis. Herpesviruses represent highly complex viruses that use a combination of these strategies, resulting in four-level hierarchical organization including a non-covalent chainmail formed by the HK97-like fold domain found in the floor region. A thorough understanding of these structures should help unlock the enigma of the emergence and evolution of dsDNA viruses and inform bioengineering efforts based on these viruses

    QCD phase diagram and the critical point

    Full text link
    The recent progress in understanding the QCD phase diagram and the physics of the QCD critical point is reviewed.Comment: 18 pages, 11 figures, for proceedings of "Finite Density QCD at Nara", July 200

    Practical Certificateless Aggregate Signatures From Bilinear Maps

    Get PDF
    Aggregate signature is a digital signature with a striking property that anyone can aggregate n individual signatures on n different messages which are signed by n distinct signers, into a single compact signature to reduce computational and storage costs. In this work, two practical certificateless aggregate signature schemes are proposed from bilinear maps. The first scheme CAS-1 reduces the costs of communication and signer-side computation but trades off the storage, while CAS-2 minimizes the storage but sacrifices the communication costs. One can choose either of the schemes by consideration of the application requirement. Compare with ID-based schemes, our schemes do not entail public key certificates as well and achieve the trust level 3, which imply the frauds of the authority are detectable. Both of the schemes are proven secure in the random oracle model by assuming the intractability of the computational Diffie-Hellman problem over the groups with bilinear maps, where the forking lemma technique is avoided

    A putative ATPase mediates RNA transcription and capping in a dsRNA virus.

    Get PDF
    mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9-3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus
    corecore