Open AccessTwo mutant alleles of mukB , a gene essential for chromosome partition in Escherichia coli
Author(s) -
Yamanaka Kunitoshi,
Mitani Tadao,
Feng Jin,
Ogura Teru,
Niki Hironori,
Hiraga Sota
Publication year - 1994
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.1574-6968.1994.tb07196.x
Subject(s) - asparagine , mutant , escherichia coli , serine , amino acid , gene , aspartic acid , residue (chemistry) , genetics , biochemistry , biology , alanine , isoleucine , chemistry , microbiology and biotechnology , leucine , enzyme
The MukB protein is essential for chromosome partitioning in Escherichia coli and consists of 1484 amino acid residues (170 kDa). We have determined the base changes at the mutated sites of the mukB106 mutant and a newly isolated mutant, mukB33 . These mutant mukB genes were each found to carry a single base‐pair transition which leads to an amino acid substitution; a serine residue at position 33 was changed to phenylalanine in the case of mukB106 , and an aspartic acid residue at position 1201 was changed to asparagine in the case of mukB33 .