Open AccessCarboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity
Author(s) -
Saleh Abu Z.M.,
Yamanaka Kunitoshi,
Niki Hironori,
Ogura Teru,
Yamazoe Mitsuyoshi,
Hiraga Sola
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08482.x
Subject(s) - escherichia coli , dna , nucleotide , biochemistry , mutant , leucine , biology , valine , mutation , binding site , amino acid , microbiology and biotechnology , chemistry , gene
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.