Mapping and characterization of mutants of the Escherichia coli cell division gene, ftsA.
Eight independent temperature-sensitive mutants of the cell division protein FtsA have been studied. They fall into two classes in terms of their behaviour at 42 degrees C and recovery at 30 degrees C. The first class shows salt-dependent temperature-sensitivity and reversible inactivation of FtsA protein at 42 degrees C. The second shows irreversible inactivation which is not prevented by salt. Recovery of the ability to divide at 30 degrees C is rapid in mutants of the first group, but is delayed for approximately a generation time in the second group. This suggests that irreversible inactivation of FtsA causes extensive damage to the division machinery. The amino acid substitutions show clustering to a limited domain of the protein, and one particular substitution is found in three of the mutants.
Robinson
A C
AC
Department of Molecular Biology, University of Edinburgh, UK.
Begg
K J
KJ
Sweeney
J
J
Condie
A
A
Donachie
W D
WD
D000483:Alleles; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology*; D001435:Bacteriophages / Q000235:genetics; D001483:Base Sequence; D002455:Cell Division; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000166:cytology / Q000235:genetics*; D005798:Genes, Bacterial; D005819:Genetic Markers; D008969:Molecular Sequence Data; D009154:Mutation; D013696:Temperature; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D005819:Genetic Markers