2014
DOI: 10.1073/pnas.1322889111
|View full text |Cite
|
Sign up to set email alerts
|

Peptidoglycan-binding protein TsaP functions in surface assembly of type IV pili

Abstract: Type IV pili (T4P) are ubiquitous and versatile bacterial cell surface structures involved in adhesion to host cells, biofilm formation, motility, and DNA uptake. In Gram-negative bacteria, T4P pass the outer membrane (OM) through the large, oligomeric, ring-shaped secretin complex. In the β-proteobacterium Neisseria gonorrhoeae, the native PilQ secretin ring embedded in OM sheets is surrounded by an additional peripheral structure, consisting of a peripheral ring and seven extending spikes. To unravel protein… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

6
91
0
1

Year Published

2015
2015
2021
2021

Publication Types

Select...
8
1

Relationship

1
8

Authors

Journals

citations
Cited by 68 publications
(98 citation statements)
references
References 72 publications
6
91
0
1
Order By: Relevance
“…Ten highly conserved proteins are known to constitute the T4PM (16, 17). PilA, the major pilin protein, contains an N-terminal hydrophobic α helix and alternates between being anchored individually in the IM or bundled with other PilA N-terminal α helices to form the central pilus core (18).…”
Section: Mapping Components In the Molecular Envelope By Imaging T4pmmentioning
confidence: 99%
“…Ten highly conserved proteins are known to constitute the T4PM (16, 17). PilA, the major pilin protein, contains an N-terminal hydrophobic α helix and alternates between being anchored individually in the IM or bundled with other PilA N-terminal α helices to form the central pilus core (18).…”
Section: Mapping Components In the Molecular Envelope By Imaging T4pmmentioning
confidence: 99%
“…Peptidoglycan-binding proteins promote pilus assembly and anchoring in the cell envelope. In the Neisseria gonorrhoeae type IVa pilus system, a peptidoglycan-binding protein anchors the apparatus in the membrane (153). In the Pseudomonas aeruginosa type IV pilus system FimV, an inner membrane protein that binds peptidoglycan is required for multimerization of PilQ (outer membrane component of the type VI pilus [154]).…”
Section: Crossing the Envelopementioning
confidence: 99%
“…178 In the case of type IV pili, TsaP is another component of the OM pore that is likely dependent on SPase processing. 179 Depending on the specific organism, the secretin of the T2SS may rely on the type II signal peptidase for processing. 180182 …”
Section: Spase Processes Components Of Multimeric Secretion Systemsmentioning
confidence: 99%