Fig. 2
- ID
- ZDB-FIG-130909-6
- Publication
- Liu et al., 2013 - A truncated Danio rerio PKZ isoform functionally interacts with eIF2alpha and inhibits protein synthesis
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Sequence analysis of DrPKZ-A and DrPKZ-B. (A) Expressions of DrPKZ-A and DrPKZ-B in zebrafish spleen. Zebrafish were challenged with ISKNV, and the spleens were collected after 6 days. RT-PCR was performed using primers covering the complete ORF. DrPKZ-A and DrPKZ-B were amplified at the predicted loci. (B) Domain organization is shown in a schematic manner. Numbers to the right represent the number of residues in DrPKZ-A, DrPKZ-B, and human PKR (HsPKR). Z-DNA binding domains (Zα and Zβ) are shown in green. Domains containing a dsRNA-binding motif are shown in light blue. The kinase domains of DrPKZ-A, DrPKZ-B (orange), and PKR (yellow) are labeled. (C) Comparison of the kinase domains from DrPKZ-A, DrPKZ-B, and HsPKR. The kinase subdomains are marked with Roman numerals as previously defined by Hanks and Hunter. The kinase insert domains (boxed in yellow), which are unique to eIF2α kinases, are located between kinase subdomains IV and V. Identical residues in the DrPKZs and in HsPKR are labeled with asterisks, and homologous residues are marked with tandem colons or single dots depending on their degree of homology. |
Reprinted from Gene, 527(1), Liu, Z.Y., Jia, K.T., Li, C., Weng, S.P., Guo, C.J., and He, J.G., A truncated Danio rerio PKZ isoform functionally interacts with eIF2alpha and inhibits protein synthesis, 292-300, Copyright (2013) with permission from Elsevier. Full text @ Gene