scholarly journals Common Evolutionary Origin of Procapsid Proteases, Phage Tail Tubes, and Tubes of Bacterial Type VI Secretion Systems

Structure ◽  
2016 ◽  
Vol 24 (11) ◽  
pp. 1928-1935 ◽  
Author(s):  
Andrei Fokine ◽  
Michael G. Rossmann
Keyword(s):  
Evolutionary Origin ◽  
Secretion Systems ◽  
Common Evolutionary Origin ◽  
Type Vi Secretion ◽  
Phage Tail ◽  
Bacterial Type

scholarly journals Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin

2009 ◽  
Vol 106 (11) ◽  
pp. 4154-4159 ◽  
Author(s):  
P. G. Leiman ◽  
M. Basler ◽  
U. A. Ramagopal ◽  
J. B. Bonanno ◽  
J. M. Sauder ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Evolutionary Origin ◽  
Common Evolutionary Origin ◽  
Type Vi Secretion ◽  
Phage Tail

scholarly journals Diverse roles of TssA‐like proteins in the assembly of bacterial type VI secretion systems

2019 ◽  
Vol 38 (18) ◽  
Author(s):  
Johannes Paul Schneider ◽  
Sergey Nazarov ◽  
Ricardo Adaixo ◽  
Martina Liuzzo ◽  
Peter David Ringel ◽  
...  
Keyword(s):  
Secretion Systems ◽  
Type Vi Secretion ◽  
Bacterial Type

scholarly journals Towards a Structural Comprehension of Bacterial Type VI Secretion Systems: Characterization of the TssJ-TssM Complex of an Escherichia coli Pathovar

2011 ◽  
Vol 7 (11) ◽  
pp. e1002386 ◽  
Author(s):  
Catarina Felisberto-Rodrigues ◽  
Eric Durand ◽  
Marie-Stéphanie Aschtgen ◽  
Stéphanie Blangy ◽  
Miguel Ortiz-Lombardia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Secretion Systems ◽  
Type Vi Secretion ◽  
Bacterial Type

scholarly journals VipA N-terminal linker and VipB-VipB interaction modulate the contraction of Type VI secretion system sheath

2017 ◽  
Author(s):  
Maximilian Brackmann ◽  
Jing Wang ◽  
Marek Basler
Keyword(s):  
Protein Translocation ◽  
Secretion System ◽  
Mass Spectrometry Analysis ◽  
Target Cells ◽  
Extended State ◽  
Type Vi Secretion System ◽  
Secretion Systems ◽  
Spectrometry Analysis ◽  
Type Vi Secretion ◽  
Bacterial Type

AbstractSecretion systems are essential for bacteria to survive and manipulate their environment. The bacterial Type VI Secretion System (T6SS) generates the force needed for protein translocation by the contraction of a long polymer called sheath, which is composed of interconnected VipA/VipB subunits forming a six-start helix. The mechanism of T6SS sheath contraction and the structure of its extended state are unknown. Here we show that elongating the N-terminal VipA linker or eliminating charge of a specific VipB residue abolished sheath contraction and delivery of effectors into target cells. The assembly of the non-contractile sheaths was dependent on the baseplate component TssE and mass-spectrometry analysis identified Hcp, VgrG and other components of the T6SS baseplate specifically associated with stable non-contractile sheaths. The ability to lock T6SS in the pre-firing state opens new possibilities for understanding its mode of action.

scholarly journals TagF-mediated repression of bacterial type VI secretion systems involves a direct interaction with the cytoplasmic protein Fha

2018 ◽  
Vol 293 (23) ◽  
pp. 8829-8842 ◽  
Author(s):  
Jer-Sheng Lin ◽  
Panayiota Pissaridou ◽  
Hsin-Hui Wu ◽  
Ming-Daw Tsai ◽  
Alain Filloux ◽  
...  
Keyword(s):  
Direct Interaction ◽  
Cytoplasmic Protein ◽  
Secretion Systems ◽  
Type Vi Secretion ◽  
Bacterial Type

scholarly journals Transferable Antibiotic Resistance Elements in Haemophilus influenzae Share a Common Evolutionary Origin with a Diverse Family of Syntenic Genomic Islands

2004 ◽  
Vol 186 (23) ◽  
pp. 8114-8122 ◽  
Author(s):  
Zaini Mohd-Zain ◽  
Sarah L. Turner ◽  
Ana M. Cerdeño-Tárraga ◽  
Andrew K. Lilley ◽  
Thomas J. Inzana ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Haemophilus Influenzae ◽  
Genomic Islands ◽  
Evolutionary Origin ◽  
Trna Genes ◽  
Secretion Systems ◽  
Accessory Gene ◽  
Common Evolutionary Origin ◽  
Wide Range ◽  
Core Genes

ABSTRACT Transferable antibiotic resistance in Haemophilus influenzae was first detected in the early 1970s. After this, resistance spread rapidly worldwide and was shown to be transferred by a large 40- to 60-kb conjugative element. Bioinformatics analysis of the complete sequence of a typical H. influenzae conjugative resistance element, ICEHin1056, revealed the shared evolutionary origin of this element. ICEHin1056 has homology to 20 contiguous sequences in the National Center for Biotechnology Information database. Systematic comparison of these homologous sequences resulted in identification of a conserved syntenic genomic island consisting of up to 33 core genes in 16 β- and γ-Proteobacteria. These diverse genomic islands shared a common evolutionary origin, insert into tRNA genes, and have diverged widely, with G+C contents ranging from 40 to 70% and amino acid homologies as low as 20 to 25% for shared core genes. These core genes are likely to account for the conjugative transfer of the genomic islands and may even encode autonomous replication. Accessory gene clusters were nestled among the core genes and encode the following diverse major attributes: antibiotic, metal, and antiseptic resistance; degradation of chemicals; type IV secretion systems; two-component signaling systems; Vi antigen capsule synthesis; toxin production; and a wide range of metabolic functions. These related genomic islands include the following well-characterized structures: SPI-7, found in Salmonella enterica serovar Typhi; PAP1 or pKLC102, found in Pseudomonas aeruginosa; and the clc element, found in Pseudomonas sp. strain B13. This is the first report of a diverse family of related syntenic genomic islands with a deep evolutionary origin, and our findings challenge the view that genomic islands consist only of independently evolving modules.

scholarly journals T6SS Mediated Stress Responses for Bacterial Environmental Survival and Host Adaptation

2021 ◽  
Vol 22 (2) ◽  
pp. 478
Author(s):  
Kai-Wei Yu ◽  
Peng Xue ◽  
Yang Fu ◽  
Liang Yang
Keyword(s):  
Protein Secretion ◽  
Stress Responses ◽  
Current Knowledge ◽  
Bacterial Species ◽  
Host Cells ◽  
Interspecies Interactions ◽  
Type Vi Secretion System ◽  
Membrane Complex ◽  
Type Vi Secretion ◽  
Bacterial Type

The bacterial type VI secretion system (T6SS) is a protein secretion apparatus widely distributed in Gram-negative bacterial species. Many bacterial pathogens employ T6SS to compete with the host and to coordinate the invasion process. The T6SS apparatus consists of a membrane complex and an inner tail tube-like structure that is surrounded by a contractile sheath and capped with a spike complex. A series of antibacterial or antieukaryotic effectors is delivered by the puncturing device consisting of a Hcp tube decorated by the VgrG/PAAR complex into the target following the contraction of the TssB/C sheath, which often leads to damage and death of the competitor and/or host cells. As a tool for protein secretion and interspecies interactions, T6SS can be triggered by many different mechanisms to respond to various physiological conditions. This review summarizes our current knowledge of T6SS in coordinating bacterial stress responses against the unfavorable environmental and host conditions.

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