Unknown

Dataset Information

0

The phosphocarrier protein HPr of the bacterial phosphotransferase system globally regulates energy metabolism by directly interacting with multiple enzymes in Escherichia coli.


ABSTRACT: The histidine-phosphorylatable phosphocarrier protein (HPr) is an essential component of the sugar-transporting phosphotransferase system (PTS) in many bacteria. Recent interactome findings suggested that HPr interacts with several carbohydrate-metabolizing enzymes, but whether HPr plays a regulatory role was unclear. Here, we provide evidence that HPr interacts with a large number of proteins in Escherichia coli We demonstrate HPr-dependent allosteric regulation of the activities of pyruvate kinase (PykF, but not PykA), phosphofructokinase (PfkB, but not PfkA), glucosamine-6-phosphate deaminase (NagB), and adenylate kinase (Adk). HPr is either phosphorylated on a histidyl residue (HPr-P) or non-phosphorylated (HPr). PykF is activated only by non-phosphorylated HPr, which decreases the PykF Khalf for phosphoenolpyruvate by 10-fold (from 3.5 to 0.36 mm), thus influencing glycolysis. PfkB activation by HPr, but not by HPr-P, resulted from a decrease in the Khalf for fructose-6-P, which likely influences both gluconeogenesis and glycolysis. Moreover, NagB activation by HPr was important for the utilization of amino sugars, and allosteric inhibition of Adk activity by HPr-P, but not by HPr, allows HPr to regulate the cellular energy charge coordinately with glycolysis. These observations suggest that HPr serves as a directly interacting global regulator of carbon and energy metabolism and probably of other physiological processes in enteric bacteria.

SUBMITTER: Rodionova IA 

PROVIDER: S-EPMC5572926 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

The phosphocarrier protein HPr of the bacterial phosphotransferase system globally regulates energy metabolism by directly interacting with multiple enzymes in <i>Escherichia coli</i>.

Rodionova Irina A IA   Zhang Zhongge Z   Mehla Jitender J   Goodacre Norman N   Babu Mohan M   Emili Andrew A   Uetz Peter P   Saier Milton H MH  

The Journal of biological chemistry 20170620 34


The histidine-phosphorylatable phosphocarrier protein (HPr) is an essential component of the sugar-transporting phosphotransferase system (PTS) in many bacteria. Recent interactome findings suggested that HPr interacts with several carbohydrate-metabolizing enzymes, but whether HPr plays a regulatory role was unclear. Here, we provide evidence that HPr interacts with a large number of proteins in <i>Escherichia coli</i> We demonstrate HPr-dependent allosteric regulation of the activities of pyru  ...[more]

Similar Datasets

| S-EPMC3436175 | biostudies-literature
| S-EPMC1357268 | biostudies-literature
| S-EPMC3390655 | biostudies-literature
| S-EPMC5031443 | biostudies-literature
| S-EPMC305802 | biostudies-literature
| S-EPMC135351 | biostudies-literature
| S-EPMC52932 | biostudies-other
| S-EPMC3409764 | biostudies-literature
| S-EPMC4996493 | biostudies-literature
| S-EPMC516805 | biostudies-literature