PMID:9721304: Difference between revisions

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<span style = 'font-size: large'> '''Draper, GC, McLennan, N, Begg, K, Masters, M and Donachie, WD'''  (1998) Only the N-terminal domain of FtsK functions in cell division.''J. Bacteriol.'' '''180''':4621-7</span>
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!align=left  |Citation
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'''Draper, GC, McLennan, N, Begg, K, Masters, M and Donachie, WD'''  (1998) Only the N-terminal domain of FtsK functions in cell division. ''J. Bacteriol.'' '''180''':4621-7
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!align=left  |Abstract
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Deletion of ftsK results in the inhibition of cell division, but this inhibition can be reversed by a plasmid carrying only the first approximately 17% of ftsK. The division block can be suppressed in most mutants by deletion of dacA, which codes for the D-alanine:D-alanine carboxypeptidase PBP5, or in all mutants by overexpression of ftsN. Overexpression of ftsK inhibits cell division and the formation of FtsZ rings. This division block is not due to the induction of either the SOS or the heat shock regulons.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9721304 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC107476 PMC107476]


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|{{TableHeadingColor}} |'''Abstract''' || Deletion of ftsK results in the inhibition of cell division, but this inhibition can be reversed by a plasmid carrying only the first approximately 17% of ftsK. The division block can be suppressed in most mutants by deletion of dacA, which codes for the D-alanine:D-alanine carboxypeptidase PBP5, or in all mutants by overexpression of ftsN. Overexpression of ftsK inhibits cell division and the formation of FtsZ rings. This division block is not due to the induction of either the SOS or the heat shock regulons.
!align=left  |Keywords
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Bacterial Proteins/chemistry; Bacterial Proteins/physiology; Base Sequence; Cell Division/physiology; DNA Primers; Escherichia coli Proteins; Membrane Proteins/chemistry; Membrane Proteins/physiology; Mutation; Plasmids; Promoter Regions, Genetic; SOS Response (Genetics); Sequence Deletion
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9721304 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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==Annotations {{HelpIcon|Help:Literature}}==
==Annotations {{HelpIcon|Help:Literature}}==
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!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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Latest revision as of 05:05, 15 September 2013

Citation

Draper, GC, McLennan, N, Begg, K, Masters, M and Donachie, WD (1998) Only the N-terminal domain of FtsK functions in cell division. J. Bacteriol. 180:4621-7

Abstract

Deletion of ftsK results in the inhibition of cell division, but this inhibition can be reversed by a plasmid carrying only the first approximately 17% of ftsK. The division block can be suppressed in most mutants by deletion of dacA, which codes for the D-alanine:D-alanine carboxypeptidase PBP5, or in all mutants by overexpression of ftsN. Overexpression of ftsK inhibits cell division and the formation of FtsZ rings. This division block is not due to the induction of either the SOS or the heat shock regulons.

Links

PubMed PMC107476

Keywords

Bacterial Proteins/chemistry; Bacterial Proteins/physiology; Base Sequence; Cell Division/physiology; DNA Primers; Escherichia coli Proteins; Membrane Proteins/chemistry; Membrane Proteins/physiology; Mutation; Plasmids; Promoter Regions, Genetic; SOS Response (Genetics); Sequence Deletion

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