Universität zu Köln

Hepp, Christof and Maier, Berenike ORCID: 0000-0001-6971-9927 (2017). Bacterial Translocation Ratchets: Shared Physical Principles with Different Molecular Implementations: How bacterial secretion systems bias Brownian motion for efficient translocation of macromolecules. Bioessays, 39 (10). HOBOKEN: WILEY. ISSN 1521-1878

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Abstract

Secretion systems enable bacteria to import and secrete large macromolecules including DNA and proteins. While most components of these systems have been identified, the molecular mechanisms of macromolecular transport remain poorly understood. Recent findings suggest that various bacterial secretion systems make use of the translocation ratchet mechanism for transporting polymers across the cell envelope. Translocation ratchets are powered by chemical potential differences generated by concentration gradients of ions or molecules that are specific to the respective secretion systems. Bacteria employ these potential differences for biasing Brownian motion of the macromolecules within the conduits of the secretion systems. Candidates for this mechanism include DNA import by the type II secretion/type IV pilus system, DNA export by the type IV secretion system, and protein export by the type I secretion system. Here, we propose that these three secretion systems employ different molecular implementations of the translocation ratchet mechanism.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Hepp, Christof UNSPECIFIED UNSPECIFIED UNSPECIFIED Maier, Berenike UNSPECIFIED orcid.org/0000-0001-6971-9927 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-216155
DOI:	10.1002/bies.201700099
Journal or Publication Title:	Bioessays
Volume:	39
Number:	10
Date:	2017
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1521-1878
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Physics > Institut für Biologische Physik
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language SINGLE-STRANDED-DNA; AGROBACTERIUM VIRE2 PROTEIN; NEISSERIA-GONORRHOEAE; ESCHERICHIA-COLI; IV PILI; NATURAL TRANSFORMATION; CRYSTAL-STRUCTURE; MULTIDRUG EFFLUX; RTX PROTEINS; HOST-CELLS Multiple languages Biochemistry & Molecular Biology; Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/21615