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Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase

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Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase. / Bandini, Giulia; Marino, Karina; Güther, M. Lucia Sampaio; Wernimont, Amy K.; Kuettel, Sabine; Qiu, Wei; Afzal, Shamshad; Kelner, Anna; Hui, Raymond; Ferguson, Michael A. J. (Lead / Corresponding author).

In: Molecular Microbiology, Vol. 85, No. 3, 2012, p. 513-534.

Research output: Contribution to journalArticle

Harvard

Bandini, G, Marino, K, Güther, MLS, Wernimont, AK, Kuettel, S, Qiu, W, Afzal, S, Kelner, A, Hui, R & Ferguson, MAJ 2012, 'Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase' Molecular Microbiology, vol 85, no. 3, pp. 513-534.

APA

Bandini, G., Marino, K., Güther, M. L. S., Wernimont, A. K., Kuettel, S., Qiu, W., Afzal, S., Kelner, A., Hui, R., & Ferguson, M. A. J. (2012). Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase. Molecular Microbiology, 85(3), 513-534doi: 10.1111/j.1365-2958.2012.08124.x

Vancouver

Bandini G, Marino K, Güther MLS, Wernimont AK, Kuettel S, Qiu W et al. Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase. Molecular Microbiology. 2012;85(3):513-534.

Author

Bandini, Giulia; Marino, Karina; Güther, M. Lucia Sampaio; Wernimont, Amy K.; Kuettel, Sabine; Qiu, Wei; Afzal, Shamshad; Kelner, Anna; Hui, Raymond; Ferguson, Michael A. J. (Lead / Corresponding author) / Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase.

In: Molecular Microbiology, Vol. 85, No. 3, 2012, p. 513-534.

Research output: Contribution to journalArticle

Bibtex - Download

@article{dc543741f6c643fa84ab5f9795a6d25c,
title = "Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase",
author = "Giulia Bandini and Karina Marino and Güther, {M. Lucia Sampaio} and Wernimont, {Amy K.} and Sabine Kuettel and Wei Qiu and Shamshad Afzal and Anna Kelner and Raymond Hui and Ferguson, {Michael A. J.}",
year = "2012",
volume = "85",
number = "3",
pages = "513--534",
journal = "Molecular Microbiology",
issn = "0950-382X",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase

A1 - Bandini,Giulia

A1 - Marino,Karina

A1 - Güther,M. Lucia Sampaio

A1 - Wernimont,Amy K.

A1 - Kuettel,Sabine

A1 - Qiu,Wei

A1 - Afzal,Shamshad

A1 - Kelner,Anna

A1 - Hui,Raymond

A1 - Ferguson,Michael A. J.

AU - Bandini,Giulia

AU - Marino,Karina

AU - Güther,M. Lucia Sampaio

AU - Wernimont,Amy K.

AU - Kuettel,Sabine

AU - Qiu,Wei

AU - Afzal,Shamshad

AU - Kelner,Anna

AU - Hui,Raymond

AU - Ferguson,Michael A. J.

PY - 2012

Y1 - 2012

N2 - The enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase (PGM) reversibly catalyse the transfer of phosphate between the C6 and C1 hydroxyl groups of mannose, N-acetylglucosamine and glucose respectively. Although genes for a candidate PMM and a PAGM enzymes have been found in the Trypanosoma brucei genome, there is, surprisingly, no candidate gene for PGM. The TbPMM and TbPAGM genes were cloned and expressed in Escherichia coli and the TbPMM enzyme was crystallized and its structure solved at 1.85Å resolution. Antibodies to the recombinant proteins localized endogenous TbPMM to glycosomes in the bloodstream form of the parasite, while TbPAGM localized to both the cytosol and glycosomes. Both recombinant enzymes were able to interconvert glucose-phosphates, as well as acting on their own definitive substrates. Analysis of sugar nucleotide levels in parasites with TbPMM or TbPAGM knocked down by RNA interference (RNAi) suggests that, in vivo, PGM activity is catalysed by both enzymes. This is the first example in any organism of PGM activity being completely replaced in this way and it explains why, uniquely, T.brucei has been able to lose its PGM gene. The RNAi data for TbPMM also showed that this is an essential gene for parasite growth. © 2012 Blackwell Publishing Ltd.

AB - The enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase (PGM) reversibly catalyse the transfer of phosphate between the C6 and C1 hydroxyl groups of mannose, N-acetylglucosamine and glucose respectively. Although genes for a candidate PMM and a PAGM enzymes have been found in the Trypanosoma brucei genome, there is, surprisingly, no candidate gene for PGM. The TbPMM and TbPAGM genes were cloned and expressed in Escherichia coli and the TbPMM enzyme was crystallized and its structure solved at 1.85Å resolution. Antibodies to the recombinant proteins localized endogenous TbPMM to glycosomes in the bloodstream form of the parasite, while TbPAGM localized to both the cytosol and glycosomes. Both recombinant enzymes were able to interconvert glucose-phosphates, as well as acting on their own definitive substrates. Analysis of sugar nucleotide levels in parasites with TbPMM or TbPAGM knocked down by RNA interference (RNAi) suggests that, in vivo, PGM activity is catalysed by both enzymes. This is the first example in any organism of PGM activity being completely replaced in this way and it explains why, uniquely, T.brucei has been able to lose its PGM gene. The RNAi data for TbPMM also showed that this is an essential gene for parasite growth. © 2012 Blackwell Publishing Ltd.

UR - http://www.scopus.com/inward/record.url?partnerID=yv4JPVwI&eid=2-s2.0-84864109063&md5=4928c1298b086a5d87dbc9a807a9e3ee

U2 - 10.1111/j.1365-2958.2012.08124.x

DO - 10.1111/j.1365-2958.2012.08124.x

M1 - Article

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 3

VL - 85

SP - 513

EP - 534

ER -

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