The PTSNtr System Globally Regulates ATP-Dependent Transporters in Rhizobium leguminosarum
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
Standard
The PTSNtr System Globally Regulates ATP-Dependent Transporters in Rhizobium leguminosarum. / Prell, Jürgen; Poole, Philip; Untiet, Verena; Karunakaran, Ramakrishnan.
Biological Nitrogen Fixation. Wiley-Blackwell, 2015. p. 349-356 (Biological Nitrogen Fixation, Vol. 1-2).Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - CHAP
T1 - The PTSNtr System Globally Regulates ATP-Dependent Transporters in Rhizobium leguminosarum
AU - Prell, Jürgen
AU - Poole, Philip
AU - Untiet, Verena
AU - Karunakaran, Ramakrishnan
PY - 2015
Y1 - 2015
N2 - Mutation of ptsP encoding EI(Ntr) of the PTS(Ntr) system in Rhizobium leguminosarum strain Rlv3841 caused a pleiotropic phenotype as observed with many bacteria. The mutant formed dry colonies and grew poorly on organic nitrogen or dicarboxylates. Most strikingly the ptsP mutant had low activity of a broad range of ATP-dependent ABC transporters. This lack of activation, which occurred post-translationally, may explain many of the pleiotropic effects. In contrast proton-coupled transport systems were not inhibited in a ptsP mutant. Regulation by PtsP also involves two copies of ptsN that code for EIIA(Ntr) , resulting in a phosphorylation cascade. As in Escherichia coli, the Rlv3841 PTS(Ntr) system also regulates K(+) homeostasis by transcriptional activation of the high-affinity ATP-dependent K(+) transporter KdpABC. This involves direct interaction of a two-component sensor regulator pair KdpDE with unphosphorylated EIIA(Ntr) . Critically, ptsP mutants, which cannot phosphorylate PtsN1 or PtsN2, had a fully activated KdpABC transporter. This is the opposite pattern from that observed with ABC transporters which apparently require phosphorylation of PtsN. These results suggest that ATP-dependent transport might be regulated via PTS(Ntr) responding to the cellular energy charge. ABC transport may be inactivated at low energy charge, conserving ATP for essential processes including K(+) homeostasis.
AB - Mutation of ptsP encoding EI(Ntr) of the PTS(Ntr) system in Rhizobium leguminosarum strain Rlv3841 caused a pleiotropic phenotype as observed with many bacteria. The mutant formed dry colonies and grew poorly on organic nitrogen or dicarboxylates. Most strikingly the ptsP mutant had low activity of a broad range of ATP-dependent ABC transporters. This lack of activation, which occurred post-translationally, may explain many of the pleiotropic effects. In contrast proton-coupled transport systems were not inhibited in a ptsP mutant. Regulation by PtsP also involves two copies of ptsN that code for EIIA(Ntr) , resulting in a phosphorylation cascade. As in Escherichia coli, the Rlv3841 PTS(Ntr) system also regulates K(+) homeostasis by transcriptional activation of the high-affinity ATP-dependent K(+) transporter KdpABC. This involves direct interaction of a two-component sensor regulator pair KdpDE with unphosphorylated EIIA(Ntr) . Critically, ptsP mutants, which cannot phosphorylate PtsN1 or PtsN2, had a fully activated KdpABC transporter. This is the opposite pattern from that observed with ABC transporters which apparently require phosphorylation of PtsN. These results suggest that ATP-dependent transport might be regulated via PTS(Ntr) responding to the cellular energy charge. ABC transport may be inactivated at low energy charge, conserving ATP for essential processes including K(+) homeostasis.
KW - ABC transport
KW - ATP
KW - Carbon metabolism
KW - Nitrogen
KW - PTS
KW - Phosphotransferase system
KW - Potassium homeostasis
U2 - 10.1002/9781119053095.ch34
DO - 10.1002/9781119053095.ch34
M3 - Book chapter
C2 - 22340847
SN - 9781119053095
T3 - Biological Nitrogen Fixation
SP - 349
EP - 356
BT - Biological Nitrogen Fixation
PB - Wiley-Blackwell
ER -
ID: 209899031