A septal chromosome segregator protein evolved into a conjugative DNA-translocator protein
Streptomycetes, Gram-positive soil bacteria well known for the production of antibiotics feature a unique conjugative DNA transfer system. In contrast to classical conjugation which is characterized by the secretion of a pilot protein covalently linked to a single-stranded DNA molecule, in Streptomy...
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Published in: | Mobile genetic elements Vol. 1; no. 3; pp. 225 - 229 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Taylor & Francis
01-09-2011
Landes Bioscience |
Subjects: | |
Online Access: | Get full text |
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Summary: | Streptomycetes, Gram-positive soil bacteria well known for the production of antibiotics feature a unique conjugative DNA transfer system. In contrast to classical conjugation which is characterized by the secretion of a pilot protein covalently linked to a single-stranded DNA molecule, in Streptomyces a double-stranded DNA molecule is translocated during conjugative transfer. This transfer involves a single plasmid encoded protein, TraB. A detailed biochemical and biophysical characterization of TraB, revealed a close relationship to FtsK, mediating chromosome segregation during bacterial cell division. TraB translocates plasmid DNA by recognizing 8-bp direct repeats located in a specific plasmid region clt. Similar sequences accidentally also occur on chromosomes and have been shown to be bound by TraB. We suggest that TraB mobilizes chromosomal genes by the interaction with these chromosomal clt-like sequences not relying on the integration of the conjugative plasmid into the chromosome. Elucidation of the molecular function of TraB highlights how nature is able to develop new machineries from other cellular processes. Whereas DNA transfer by classical conjugation is done by specialized type IV protein secretion systems, for the conjugative DNA transfer in Streptomyces a chromosome segregation system was rebuild. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current affiliation: Centre de Biochimie Structurale; CNRS UMR 5048-UM 1-INSERM UMR 554; Montpellier, France |
ISSN: | 2159-2543 2159-256X 2159-256X |
DOI: | 10.4161/mge.1.3.18066 |