Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10770462 | Biochemical and Biophysical Research Communications | 2005 | 7 Pages |
Abstract
Gp1, the product of one of the essential genes of Ï29 replication, is an RNA binding protein and self-associates to form large complexes. Furthermore, gp1 suppresses the synthesis of Ï29 DNA polymerase and primer protein in the post-transcriptional process. In this report, we have employed seven variants with single amino acid substitutions to analyze the self-assembly of gp1. Using chemical cross-linking and sedimentation assays, amino acid substitutions within the predicted coiled-coil or hydrophobic region were shown to strongly affect the formation of large complexes, suggesting that these two regions were required for the self-assembly of gp1. The self-association of gp1 was suggested to be necessary for the efficient binding to RNA and the translational repression.
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Authors
Kazuya Hashiyama, Ari Takeuchi, Osamu Makino,