RRC ID |
56366
|
Author |
Jiang N, Tang L, Xie R, Li Z, Burkinshaw B, Liang X, Sosa D, Aravind L, Dong T, Zhang D, Zheng J.
|
Title |
Vibrio parahaemolyticus RhsP represents a widespread group of pro-effectors for type VI secretion systems.
|
Journal |
Nat Commun
|
Abstract |
Type VI secretion systems (T6SSs) translocate effector proteins, such as Rhs toxins, to eukaryotic cells or prokaryotic competitors. All T6SS Rhs-type effectors characterized thus far contain a PAAR motif or a similar structure. Here, we describe a T6SS-dependent delivery mechanism for a subset of Rhs proteins that lack a PAAR motif. We show that the N-terminal Rhs domain of protein RhsP (or VP1517) from Vibrio parahaemolyticus inhibits the activity of the C-terminal DNase domain. Upon auto-proteolysis, the Rhs fragment remains inside the cells, and the C-terminal region interacts with PAAR2 and is secreted by T6SS2; therefore, RhsP acts as a pro-effector. Furthermore, we show that RhsP contributes to the control of certain "social cheaters" (opaR mutants). Genes encoding proteins with similar Rhs and PAAR-interacting domains, but diverse C-terminal regions, are widely distributed among Vibrio species.
|
Volume |
9(1)
|
Pages |
3899
|
Published |
2018-9-25
|
DOI |
10.1038/s41467-018-06201-5
|
PII |
10.1038/s41467-018-06201-5
|
PMID |
30254227
|
PMC |
PMC6156420
|
MeSH |
Amino Acid Motifs / genetics
Amino Acid Sequence
Bacterial Proteins / chemistry
Bacterial Proteins / genetics*
Bacterial Proteins / metabolism
Bacterial Toxins / chemistry
Bacterial Toxins / genetics*
Bacterial Toxins / metabolism
Binding Sites / genetics
Mutagenesis, Site-Directed
Protein Binding
Protein Domains
Sequence Homology, Amino Acid
Type VI Secretion Systems / genetics*
Type VI Secretion Systems / metabolism
Vibrio parahaemolyticus / genetics*
Vibrio parahaemolyticus / metabolism
|
IF |
11.878
|
Times Cited |
7
|
Resource |
Pathogenic bacteria |
JNBP_30766(RIMD 2210633) |