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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-1-14
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pubmed:abstractText |
In prokaryotes, the toxin-antitoxin systems are thought to play important roles in growth regulation under stress conditions. In the E. coli MazE-MazF system, MazF toxin functions as an mRNA interferase cleaving mRNAs at ACA sequences to inhibit protein synthesis leading to cell growth arrest. Myxococcus xanthus is a bacterium displaying multicellular fruiting body development during which approximately 80% of cells undergo obligatory cell lysis. Here, we demonstrate that M. xanthus has a solitary mazF gene that lacks a cotranscribed antitoxin gene. The mazF deletion results in elimination of the obligatory cell death during development causing dramatic reduction in spore formation. Surprisingly, MrpC, a key developmental regulator, functions as a MazF antitoxin and a mazF transcription activator. Transcription of mrpC and mazF is negatively regulated via MrpC phosphorylation by a Ser/Thr kinase cascade. These findings reveal the regulated deployment of a toxin gene for developmental programmed cell death in bacteria.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MazF protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/MrpC protein, Myxococcus xanthus,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
132
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
55-66
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pubmed:meshHeading |
pubmed-meshheading:18191220-Amino Acid Sequence,
pubmed-meshheading:18191220-Apoptosis,
pubmed-meshheading:18191220-Apoptosis Regulatory Proteins,
pubmed-meshheading:18191220-Bacterial Proteins,
pubmed-meshheading:18191220-Base Sequence,
pubmed-meshheading:18191220-Cell Cycle Proteins,
pubmed-meshheading:18191220-Cell Division,
pubmed-meshheading:18191220-Cell Proliferation,
pubmed-meshheading:18191220-DNA-Binding Proteins,
pubmed-meshheading:18191220-Endoribonucleases,
pubmed-meshheading:18191220-Escherichia coli Proteins,
pubmed-meshheading:18191220-Gene Deletion,
pubmed-meshheading:18191220-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18191220-Molecular Sequence Data,
pubmed-meshheading:18191220-Myxococcus,
pubmed-meshheading:18191220-Phosphorylation,
pubmed-meshheading:18191220-RNA, Messenger,
pubmed-meshheading:18191220-Sequence Homology, Amino Acid,
pubmed-meshheading:18191220-Spheroids, Cellular,
pubmed-meshheading:18191220-Transcription, Genetic,
pubmed-meshheading:18191220-Transcription Factors
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pubmed:year |
2008
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pubmed:articleTitle |
MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development.
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pubmed:affiliation |
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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