Effects of single amino acid substitutions at the predicted coiled-coil or hydrophobic region on the self-assembly of ϕ29 replication protein, gp1

Gp1, the product of one of the essential genes of ϕ29 replication, is an RNA binding protein and self-associates to form large complexes. Furthermore, gp1 suppresses the synthesis of ϕ29 DNA polymerase and primer protein in the post-transcriptional process. In this report, we have employed seven var...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-06, Vol.331 (4), p.1310-1316
Main Authors: Hashiyama, Kazuya, Takeuchi, Ari, Makino, Osamu
Format: Article
Language:English
Subjects:
Chemical cross-linking
Coiled-coil structure
Glycerol gradient sedimentation
Hydrophobic region
In vitro translation
RNA binding protein
Self-assembly
Single amino acid substitution
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Summary:Gp1, the product of one of the essential genes of ϕ29 replication, is an RNA binding protein and self-associates to form large complexes. Furthermore, gp1 suppresses the synthesis of ϕ29 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.04.056