Abstract
We previously reported that the Vibrio parahaemolyticus pvsABCDE and psuA-pvuABCDE operons are involved in the biosynthesis and transport of its own siderophore, vibrioferrin (VF). Of these, psuA and pvuA encode TonB-dependent outer-membrane proteins (OMPs). Although pvuA was characterized as the ferric vibrioferrin receptor gene, the role of the psuA product remains unknown. In this study, a growth assay of isogenic psuA, pvuA, and psuA-pvuA double-deletion mutants followed by complementation of the double-deletion mutant with psuA or pvuA was used to identify psuA as a gene encoding an OMP involved in the uptake of ferric VF. Thus, psuA and pvuA were renamed pvuA1 and pvuA2, respectively. Moreover, we clarified the TonB specificities of PvuA1 and PvuA2, because V. parahaemolyticus has three sets of the TonB systems. The triple deletion of pvuA1, tonB1, and tonB2, and the double deletion of pvuA2 and tonB2 resulted in the complete loss of growth promotion by VF. This finding indicates that the energy required for PvuA1 and PvuA2 to transport ferric VF across the outer membrane is provided by the TonB2 system and by both the TonB1 and TonB2 systems, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 73-79 |
| Number of pages | 7 |
| Journal | FEMS Microbiology Letters |
| Volume | 324 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Nov 2011 |
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Keywords
- Ferric vibrioferrin receptor
- Siderophore
- TonB-dependent outer-membrane receptor
- Vibrio parahaemolyticus
- Vibrioferrin-utilization gene cluster
ASJC Scopus subject areas
- Microbiology
- Genetics
- Molecular Biology
Cite this
The Vibrio parahaemolyticus pvuA1 gene (formerly termed psuA) encodes a second ferric vibrioferrin receptor that requires tonB2. / Tanabe, Tomotaka; Funahashi, Tatsuya; Okajima, Noriyuki; Nakao, Hiroshi; Takeuchi, Yasuo; Miyamoto, Katsushiro; Tsujibo, Hiroshi; Yamamoto, Shigeo.
In: FEMS Microbiology Letters, Vol. 324, No. 1, 11.2011, p. 73-79.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The Vibrio parahaemolyticus pvuA1 gene (formerly termed psuA) encodes a second ferric vibrioferrin receptor that requires tonB2
AU - Tanabe, Tomotaka
AU - Funahashi, Tatsuya
AU - Okajima, Noriyuki
AU - Nakao, Hiroshi
AU - Takeuchi, Yasuo
AU - Miyamoto, Katsushiro
AU - Tsujibo, Hiroshi
AU - Yamamoto, Shigeo
PY - 2011/11
Y1 - 2011/11
N2 - We previously reported that the Vibrio parahaemolyticus pvsABCDE and psuA-pvuABCDE operons are involved in the biosynthesis and transport of its own siderophore, vibrioferrin (VF). Of these, psuA and pvuA encode TonB-dependent outer-membrane proteins (OMPs). Although pvuA was characterized as the ferric vibrioferrin receptor gene, the role of the psuA product remains unknown. In this study, a growth assay of isogenic psuA, pvuA, and psuA-pvuA double-deletion mutants followed by complementation of the double-deletion mutant with psuA or pvuA was used to identify psuA as a gene encoding an OMP involved in the uptake of ferric VF. Thus, psuA and pvuA were renamed pvuA1 and pvuA2, respectively. Moreover, we clarified the TonB specificities of PvuA1 and PvuA2, because V. parahaemolyticus has three sets of the TonB systems. The triple deletion of pvuA1, tonB1, and tonB2, and the double deletion of pvuA2 and tonB2 resulted in the complete loss of growth promotion by VF. This finding indicates that the energy required for PvuA1 and PvuA2 to transport ferric VF across the outer membrane is provided by the TonB2 system and by both the TonB1 and TonB2 systems, respectively.
AB - We previously reported that the Vibrio parahaemolyticus pvsABCDE and psuA-pvuABCDE operons are involved in the biosynthesis and transport of its own siderophore, vibrioferrin (VF). Of these, psuA and pvuA encode TonB-dependent outer-membrane proteins (OMPs). Although pvuA was characterized as the ferric vibrioferrin receptor gene, the role of the psuA product remains unknown. In this study, a growth assay of isogenic psuA, pvuA, and psuA-pvuA double-deletion mutants followed by complementation of the double-deletion mutant with psuA or pvuA was used to identify psuA as a gene encoding an OMP involved in the uptake of ferric VF. Thus, psuA and pvuA were renamed pvuA1 and pvuA2, respectively. Moreover, we clarified the TonB specificities of PvuA1 and PvuA2, because V. parahaemolyticus has three sets of the TonB systems. The triple deletion of pvuA1, tonB1, and tonB2, and the double deletion of pvuA2 and tonB2 resulted in the complete loss of growth promotion by VF. This finding indicates that the energy required for PvuA1 and PvuA2 to transport ferric VF across the outer membrane is provided by the TonB2 system and by both the TonB1 and TonB2 systems, respectively.
KW - Ferric vibrioferrin receptor
KW - Siderophore
KW - TonB-dependent outer-membrane receptor
KW - Vibrio parahaemolyticus
KW - Vibrioferrin-utilization gene cluster
UR - http://www.scopus.com/inward/record.url?scp=80053510605&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80053510605&partnerID=8YFLogxK
U2 - 10.1111/j.1574-6968.2011.02389.x
DO - 10.1111/j.1574-6968.2011.02389.x
M3 - Article
C2 - 22092766
AN - SCOPUS:80053510605
VL - 324
SP - 73
EP - 79
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -