Abstract:
:Cell division in Caulobacter crescentus involves constriction and fission of the inner membrane (IM) followed about 20 min later by fission of the outer membrane (OM) and daughter cell separation. In contrast to Escherichia coli, the Caulobacter Tol-Pal complex is essential. Cryo-electron microscopy images of the Caulobacter cell envelope exhibited outer membrane disruption, and cells failed to complete cell division in TolA, TolB, or Pal mutant strains. In wild-type cells, components of the Tol-Pal complex localize to the division plane in early predivisional cells and remain predominantly at the new pole of swarmer and stalked progeny upon completion of division. The Tol-Pal complex is required to maintain the position of the transmembrane TipN polar marker, and indirectly the PleC histidine kinase, at the cell pole, but it is not required for the polar maintenance of other transmembrane and membrane-associated polar proteins tested. Coimmunoprecipitation experiments show that both TolA and Pal interact directly or indirectly with TipN. We propose that disruption of the trans-envelope Tol-Pal complex releases TipN from its subcellular position. The Caulobacter Tol-Pal complex is thus a key component of cell envelope structure and function, mediating OM constriction at the final step of cell division as well as the positioning of a protein localization factor.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Yeh YC,Comolli LR,Downing KH,Shapiro L,McAdams HHdoi
10.1128/JB.00607-10subject
Has Abstractpub_date
2010-10-01 00:00:00pages
4847-58issue
19eissn
0021-9193issn
1098-5530pii
JB.00607-10journal_volume
192pub_type
杂志文章abstract::Fourteen bacterial strains of marine origin, which formed colonies containing crystals of a blue-black pigment, were submitted to a morphological, physiological, and nutritional characterization. The results indicated that these organisms form a new species of the genus Beneckea. ...
journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.108.3.1380-1383.1971
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abstract::Uptake of cobalamins and iron chelates in Escherichia coli K-12 is dependent on specific outer membrane transport proteins and the energy-coupling function provided by the TonB protein. The btuB product is the outer membrane receptor for cobalamins, bacteriophage BF23, and the E colicins. A short sequence near the ami...
journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1128/JB.123.3.862-870.1975
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1994-06-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1984-05-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1997-04-01 00:00:00
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1973-02-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:2003-12-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:2011-10-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.00404-07
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