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The mutL repair gene of Escherichia coli K‐12 forms a superoperon with a gene encoding a new cell‐wall amidase
Author(s) -
Tsui HoChing Tiffany,
Zhao Genshi,
Feng Gang,
Leung HonChlu Eastwood,
Winkler Malcolm E.
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb00300.x
Subject(s) - biology , escherichia coli , amidase , gene , microbiology and biotechnology , bacillus subtilis , autolysin , genetics , peptidoglycan , bacteria
Summary We report a molecular genetic analysis of the region Immediately upstream from the Escherichia coli mutL DNA repair gene at 94.8 min. An open reading frame ending 9bp upstream from the start of mutL corresponds to a 48kDa polypeptide detected previously in minicells. The predicted amino acid sequence of this 48kDa polypeptide shows homology to the major N‐acetylmuramoyl‐L‐alanine amidase autolysin of Bacillus subtilis , a known amidase of Bacillus licheniformis , and the product of a Salmonella typhimurium gene that maps near SO min. Insertions in this upstream gene, which we named AmiB , or in mutL did not affect cell shape or viability; however, overexpression of the AmiB potypeptide caused ceil lysis, hypersensitivity to osmotic shock and treatment with water, and temporary autolysis by low levels of antibiotics, which are all consistent with AmiB acting as a cell‐wall hydrolase. Analysis of chromosomal transcription demonstrated that amiB forms a complex operon with mutL and two additional upstream genes. mutL transcripts also originated from an internal promoter, designated P mutL , located in amiB 312bp upstream from the translational start of mutL. Together, these results suggest that E. coli contains a second amidase possibly involved in cell‐wall hydrolysis, septation, or recycling, and that transcription of this amidase is directly linked to a gene central for DNA repair.