Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity.
The purified MukB protein of Escherichia coli has DNA binding activity and nucleotide binding activity. We have isolated a mutation, mukB1013, causing a substitution of valine at position 1379 to leucine. This mutant MukB protein was defective for DNA binding, while the ATP binding activity remained unaffected. A truncated MukB protein that is short of 109 amino acids from the C-terminus failed to bind DNA.
Saleh
A Z
AZ
Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan.
Yamanaka
K
K
Niki
H
H
Ogura
T
T
Yamazoe
M
M
Hiraga
S
S
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D002868:Chromosomal Proteins, Non-Histone; D017931:DNA Primers / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D016297:Mutagenesis, Site-Directed; D010641:Phenotype; D010957:Plasmids / Q000235:genetics; D017354:Point Mutation; D017384:Sequence Deletion; D013696:Temperature
D001426:Bacterial Proteins; D002868:Chromosomal Proteins, Non-Histone; D017931:DNA Primers; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C067035:MukB protein, E coli; D000255:Adenosine Triphosphate