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N-Terminal domain of Bombyx mori fibroin mediates the assembly of silk in response to pH decrease.
- Yongxing He, Nan-nan Zhang, +6 authors Cong-Zhao Zhou
- Chemistry, Medicine
- Journal of molecular biology
- 4 May 2012
It is suggested that FibNT functions as a pH-responsive self-assembly module that could prevent premature β-sheet formation at neutral pH yet could initiate fibroin assembly as pH decreases along the lumen of the posterior silk gland to the anterior silk gland. Expand
Structural basis for receptor recognition and pore formation of a zebrafish aerolysin‐like protein
Structural analyses combined with computational simulations and biochemical assays suggest a pore‐forming process with an activation mechanism distinct from the previously characterized bacterial members, and Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish‐specific defense molecule. Expand
A DNA2 Homolog Is Required for DNA Damage Repair, Cell Cycle Regulation, and Meristem Maintenance in Plants1[OPEN]
The results suggest that JHS1 plays an important role in DNA replication and damage repair, meristem maintenance, and development in plants. Expand
Type III-A CRISPR-Cas Csm Complexes: Assembly, Periodic RNA Cleavage, DNase Activity Regulation, and Autoimmunity.
- N. Jia, C. Y. Mo, Chongyuan Wang, E. Eng, L. Marraffini, D. Patel
- Biology, Medicine
- Molecular cell
- 17 January 2019
Structural findings provide insights into CsmcrRNA complex assembly, mechanisms underlying RNA targeting and site-specific periodic cleavage, regulation of DNase cleavage activity, and autoimmunity suppression. Expand
Structural insights into the coordination of plastid division by the ARC6–PDV2 complex
The crystal structure of the intermembrane space region of the ARC6–PDV2 complex is solved and reveals that PDV2-induced dimerization of ARC6 plays a critical role in chloroplast division and provides insights into the coordination mechanism of the internal and external plastid division machineries. Expand
CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA4 Cleavage with ApA>p Formation Terminating RNase Activity.
- N. Jia, Roger A. Jones, G. Yang, O. Ouerfelli, D. Patel
- Biology, Medicine
- Molecular cell
- 5 September 2019
It is demonstrated that the Csm6 CARF domain is a ring nuclease, whereby bound cA4 is stepwise cleaved initially to ApApApA >p and subsequently to ApA>p in its CARFdomain-binding pocket, with such cleavage bursts using a timer mechanism to regulate the RNase activity of the CSm6 HEPN domain. Expand
A phage-encoded anti-CRISPR enables complete evasion of type VI-A CRISPR-Cas immunity
A listeriaphage encoding an anti-CRISPR protein that inactivates the type VI-A CRISPR system of Listeria seeligeri is described and it is found that AcrVIA1 interacts with the guide-exposed face of Cas13a, preventing access to the target RNA and the conformational changes required for nuclease activation. Expand
Second Messenger cA4 Formation within the Composite Csm1 Palm Pocket of Type III-A CRISPR-Cas Csm Complex and Its Release Path.
Structural results from cryo-EM and X-ray studies on multi-subunit Thermococcus onnurineus Csm effector ternary complexes are combined with published functional studies to highlight mechanistic insights into the role of the CSm effector complex in mediating the cAn signaling pathway. Expand
Effect of site-directed PEGylation of trichosanthin on its biological activity, immunogenicity, and pharmacokinetics.
It is worthwhile to further explore the potential application of the PEGylated TCS as a better therapeutic agent for AIDS and tumor. Expand
Crystal structure of juvenile hormone epoxide hydrolase from the silkworm Bombyx mori
Structural analyses together with molecular simulation reveal insights into the specific binding of JH in the active-site pocket and increase the understanding of the substrate recognition and catalysis of mEHs and might help the design ofJH-derived pesticides. Expand