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Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli

Research output: Contribution to journalArticlepeer-review

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Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli. / Nurmohamed, S.; Vincent, H.; Titman, C.; Chandran, V.; Pears, M.; Du, D.; Griffin, J.; Callaghan, Anastasia; Luisi, B.

In: The Journal of Biological Chemistry, Vol. 286, 04.2011, p. 14315-14323.

Research output: Contribution to journalArticlepeer-review

Harvard

Nurmohamed, S, Vincent, H, Titman, C, Chandran, V, Pears, M, Du, D, Griffin, J, Callaghan, A & Luisi, B 2011, 'Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli', The Journal of Biological Chemistry, vol. 286, pp. 14315-14323. https://doi.org/10.1074/jbc.M110.200741

APA

Nurmohamed, S., Vincent, H., Titman, C., Chandran, V., Pears, M., Du, D., Griffin, J., Callaghan, A., & Luisi, B. (2011). Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli. The Journal of Biological Chemistry, 286, 14315-14323. https://doi.org/10.1074/jbc.M110.200741

Vancouver

Nurmohamed S, Vincent H, Titman C, Chandran V, Pears M, Du D et al. Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli. The Journal of Biological Chemistry. 2011 Apr;286:14315-14323. https://doi.org/10.1074/jbc.M110.200741

Author

Nurmohamed, S. ; Vincent, H. ; Titman, C. ; Chandran, V. ; Pears, M. ; Du, D. ; Griffin, J. ; Callaghan, Anastasia ; Luisi, B. / Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli. In: The Journal of Biological Chemistry. 2011 ; Vol. 286. pp. 14315-14323.

Bibtex

@article{e531bf21118845058d58ec317f83ffa3,
title = "Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli",
abstract = "RNA turnover is an essential element of cellular homeostasis and response to environmental change. Whether the ribonucleases that mediate RNA turnover can respond to cellular metabolic status is an unresolved question. Here we present evidence that the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity. An E. coli strain that requires PNPase for viability has suppressed growth in the presence of increased citrate concentration. Transcriptome analysis reveals a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. In vitro, citrate directly binds and modulates PNPase activity, as predicted by crystallographic data. Binding of metal-chelated citrate in the active site at physiological concentrations appears to inhibit enzyme activity. However, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity. Mutagenesis data confirmed a potential role of this vestigial site as an allosteric binding pocket that recognizes metal-free citrate. Collectively, these findings suggest that RNA degradative pathways communicate with central metabolism. This communication appears to be part of a feedback network that may contribute to global regulation of metabolism and cellular energy efficiency.",
author = "S. Nurmohamed and H. Vincent and C. Titman and V. Chandran and M. Pears and D. Du and J. Griffin and Anastasia Callaghan and B. Luisi",
year = "2011",
month = apr,
doi = "10.1074/jbc.M110.200741",
language = "English",
volume = "286",
pages = "14315--14323",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

RIS

TY - JOUR

T1 - Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli

AU - Nurmohamed, S.

AU - Vincent, H.

AU - Titman, C.

AU - Chandran, V.

AU - Pears, M.

AU - Du, D.

AU - Griffin, J.

AU - Callaghan, Anastasia

AU - Luisi, B.

PY - 2011/4

Y1 - 2011/4

N2 - RNA turnover is an essential element of cellular homeostasis and response to environmental change. Whether the ribonucleases that mediate RNA turnover can respond to cellular metabolic status is an unresolved question. Here we present evidence that the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity. An E. coli strain that requires PNPase for viability has suppressed growth in the presence of increased citrate concentration. Transcriptome analysis reveals a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. In vitro, citrate directly binds and modulates PNPase activity, as predicted by crystallographic data. Binding of metal-chelated citrate in the active site at physiological concentrations appears to inhibit enzyme activity. However, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity. Mutagenesis data confirmed a potential role of this vestigial site as an allosteric binding pocket that recognizes metal-free citrate. Collectively, these findings suggest that RNA degradative pathways communicate with central metabolism. This communication appears to be part of a feedback network that may contribute to global regulation of metabolism and cellular energy efficiency.

AB - RNA turnover is an essential element of cellular homeostasis and response to environmental change. Whether the ribonucleases that mediate RNA turnover can respond to cellular metabolic status is an unresolved question. Here we present evidence that the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity. An E. coli strain that requires PNPase for viability has suppressed growth in the presence of increased citrate concentration. Transcriptome analysis reveals a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. In vitro, citrate directly binds and modulates PNPase activity, as predicted by crystallographic data. Binding of metal-chelated citrate in the active site at physiological concentrations appears to inhibit enzyme activity. However, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity. Mutagenesis data confirmed a potential role of this vestigial site as an allosteric binding pocket that recognizes metal-free citrate. Collectively, these findings suggest that RNA degradative pathways communicate with central metabolism. This communication appears to be part of a feedback network that may contribute to global regulation of metabolism and cellular energy efficiency.

U2 - 10.1074/jbc.M110.200741

DO - 10.1074/jbc.M110.200741

M3 - Article

VL - 286

SP - 14315

EP - 14323

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

ER -

ID: 57269