Mutual suppression of mukB and seqA phenotypes might arise from their opposing influences on the Escherichia coli nucleoid structure.
A strain of Escherichia coli in which both the seqA and mukB genes were inactivated displayed partial suppressions of their individual phenotypes. Temperature sensitivity, anucleate cell production and poor nucleoid folding seen in the mukB strain were suppressed by the seqA null mutation, whereas filamentation, asymmetric septation and compact folding of the nucleoids observed in the seqA strain were suppressed by inactivation of the mukB gene function. However, the asynchronous initiation of chromosome replication in the seqA strain was not reversed in the mukBseqA double mutant. Membrane-associated nucleoids were isolated from the wild-type, mukB, seqA and mukBseqA strains and their sedimentation rates were compared under identical conditions. Whereas the mukB mutation caused unfolding of the nucleoid, the seqA mutation led to a more compact packaging of the chromosome. The mukBseqA double mutant regained the wild-type nucleoid organization as revealed from its rate of sedimentation. Microscopic appearances of the nucleoids were consistent with the sedimentation profiles. The mukB mutant was oversensitive to novobiocin and this susceptibility was suppressed in the mukBseqA strain, suggesting possible roles of MukB and SeqA in maintaining chromosome topology. The mutual phenotypic suppression of mukB and seqA alleles thus suggests that these genes have opposing influences on the organization of the bacterial nucleoid.
Weitao
T
T
Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, SE-751 24 Uppsala, Sweden.
Nordström
K
K
Dasgupta
S
S
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D002455:Cell Division / Q000235:genetics; D002498:Centrifugation / Q000379:methods; D002868:Chromosomal Proteins, Non-Histone; D002876:Chromosomes, Bacterial / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure*; D004261:DNA Replication; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology* / Q000187:drug effects / Q000235:genetics*; D029968:Escherichia coli Proteins; D005434:Flow Cytometry; D008856:Microscopy, Fluorescence; D009675:Novobiocin / Q000494:pharmacology; D010641:Phenotype; D013489:Suppression, Genetic; D014157:Transcription Factors
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C067035:MukB protein, E coli; C089746:SeqA protein, E coli; D014157:Transcription Factors; D009675:Novobiocin