T
Teru Ogura
Researcher at Kyoto University
Publications - 11
Citations - 1439
Teru Ogura is an academic researcher from Kyoto University. The author has contributed to research in topics: Plasmid & Mutant. The author has an hindex of 9, co-authored 11 publications receiving 1407 citations. Previous affiliations of Teru Ogura include National Institutes of Health.
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Chromosome Partitioning inEscherichia coli: NovelMutants Producing Anucleate Cells
TL;DR: In this article, the authors have isolated a type of Escherichia coli mutants which formed anucleate cells, named mukA1, by using newly developed techniques and found that the mutant is defective in the chromosome positioning at regular intracellular positions and fails frequently to partition the replicated daughter chromosomes into both daughter cells.
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Partition mechanism of F plasmid: Two plasmid gene-encoded products and a cis-acting region are involved in partition
Teru Ogura,Sota Hiraga +1 more
TL;DR: Plasmids that replicate using the replication origin of the E. coli chromosome are not stably inherited through cell division, but can be stabilized by joining with a particular segment of F plasmid that presumably provides the partition function.
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Effects of the ccd function of the F plasmid on bacterial growth
A Jaffé,Teru Ogura,Sota Hiraga +2 more
TL;DR: Results are presented suggesting that plasmid-containing cells are viable and continue to divide, whereas plasmids-free segregants are nonviable and form filaments after a few residual divisions, with DNA synthesis reduced or arrested in the filaments.
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Structure and function of the F plasmid genes essential for partitioning.
TL;DR: Analysis of deletions in the sopC region showed that the direct repeats play an important role in plasmid partition and IncD incompatibility.
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Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter
TL;DR: The loss of ftsH function enhances translocation of normally anchored protein segments and retards that of normally translocated proteins, suggesting that FtsH participates in assembly of proteins into and through the membrane.