The C-terminal residues of the 2b protein of Cucumber mosaic virus are important for efficient expression in Escherichia coli and DNA-binding.
The RNA silencing suppressor 2b protein of Cucumber mosaic virus (CMV) is difficult to produce in Escherichia coli. We compared two CMV 2b proteins that differ in their toxicity against E. coli and found that the acidic amino acid residues in the C-terminal significantly affected the toxicity and expression level of the protein in E. coli. In addition, in a DNA-binding assay, 2b had the ability to bind to DNA, and this ability was affected by the charge on the C-terminal residues of 2b. We concluded that the C-terminal residues were important for 2b's DNA-binding ability, which may partly explain the toxicity of the protein.
Sueda
Kae
K
Laboratory of Cell Biology and Manipulation, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.
Shimura
Hanako
H
Meguro
Ayano
A
Uchida
Takeshi
T
Inaba
Jun-ichi
J
Masuta
Chikara
C
D000595:Amino Acid Sequence; D004247:DNA / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000235:genetics / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
C404227:2b protein, cucumber mosaic virus; D014764:Viral Proteins; D004247:DNA