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Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum. / Pullen, Timothy J.; Ginger, Michael L.; Gaskell, Simon J. et al.
In: Molecular Biology of the Cell, Vol. 15, No. 7, 07.2004, p. 3257-3265.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Pullen, TJ, Ginger, ML, Gaskell, SJ & Gull, K 2004, 'Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum.', Molecular Biology of the Cell, vol. 15, no. 7, pp. 3257-3265. https://doi.org/10.1091/mbc.E04-03-0217

APA

Pullen, T. J., Ginger, M. L., Gaskell, S. J., & Gull, K. (2004). Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum. Molecular Biology of the Cell, 15(7), 3257-3265. https://doi.org/10.1091/mbc.E04-03-0217

Vancouver

Pullen TJ, Ginger ML, Gaskell SJ, Gull K. Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum. Molecular Biology of the Cell. 2004 Jul;15(7):3257-3265. doi: 10.1091/mbc.E04-03-0217

Author

Pullen, Timothy J. ; Ginger, Michael L. ; Gaskell, Simon J. et al. / Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum. In: Molecular Biology of the Cell. 2004 ; Vol. 15, No. 7. pp. 3257-3265.

Bibtex

@article{e10206998ec34a19b8b284273940b28a,
title = "Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum.",
abstract = "The eukaryotic flagellum is a large structure into which specific constituent proteins must be targeted, transported and assembled after their synthesis in the cytoplasm. Using Trypanosoma brucei and a proteomic approach, we have identified and characterized a novel set of adenylate kinase proteins that are localized to the flagellum. These proteins represent unique isoforms that are targeted to the flagellum by an N-terminal extension to the protein and are incorporated into an extraaxonemal structure (the paraflagellar rod). We show that the N-terminal extension is both necessary for isoform location in the flagellum and sufficient for targeting of a green fluorescent protein reporter protein to the flagellum. Moreover, these N-terminal extension sequences are conserved in evolution and we find that they allow the identification of novel adenylate kinases in the genomes of humans and worms. Given the existence of specific isoforms of certain central metabolic enzymes, and targeting sequences for these isoforms, we suggest that these isoforms form part of a complex, {"}solid-phase{"} metabolic capability that is built into the eukaryotic flagellum.",
author = "Pullen, {Timothy J.} and Ginger, {Michael L.} and Gaskell, {Simon J.} and Keith Gull",
year = "2004",
month = jul,
doi = "10.1091/mbc.E04-03-0217",
language = "English",
volume = "15",
pages = "3257--3265",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "7",

}

RIS

TY - JOUR

T1 - Protein Targeting of an Unusual, Evolutionarily Conserved Adenylate Kinase to a Eukaryotic Flagellum.

AU - Pullen, Timothy J.

AU - Ginger, Michael L.

AU - Gaskell, Simon J.

AU - Gull, Keith

PY - 2004/7

Y1 - 2004/7

N2 - The eukaryotic flagellum is a large structure into which specific constituent proteins must be targeted, transported and assembled after their synthesis in the cytoplasm. Using Trypanosoma brucei and a proteomic approach, we have identified and characterized a novel set of adenylate kinase proteins that are localized to the flagellum. These proteins represent unique isoforms that are targeted to the flagellum by an N-terminal extension to the protein and are incorporated into an extraaxonemal structure (the paraflagellar rod). We show that the N-terminal extension is both necessary for isoform location in the flagellum and sufficient for targeting of a green fluorescent protein reporter protein to the flagellum. Moreover, these N-terminal extension sequences are conserved in evolution and we find that they allow the identification of novel adenylate kinases in the genomes of humans and worms. Given the existence of specific isoforms of certain central metabolic enzymes, and targeting sequences for these isoforms, we suggest that these isoforms form part of a complex, "solid-phase" metabolic capability that is built into the eukaryotic flagellum.

AB - The eukaryotic flagellum is a large structure into which specific constituent proteins must be targeted, transported and assembled after their synthesis in the cytoplasm. Using Trypanosoma brucei and a proteomic approach, we have identified and characterized a novel set of adenylate kinase proteins that are localized to the flagellum. These proteins represent unique isoforms that are targeted to the flagellum by an N-terminal extension to the protein and are incorporated into an extraaxonemal structure (the paraflagellar rod). We show that the N-terminal extension is both necessary for isoform location in the flagellum and sufficient for targeting of a green fluorescent protein reporter protein to the flagellum. Moreover, these N-terminal extension sequences are conserved in evolution and we find that they allow the identification of novel adenylate kinases in the genomes of humans and worms. Given the existence of specific isoforms of certain central metabolic enzymes, and targeting sequences for these isoforms, we suggest that these isoforms form part of a complex, "solid-phase" metabolic capability that is built into the eukaryotic flagellum.

U2 - 10.1091/mbc.E04-03-0217

DO - 10.1091/mbc.E04-03-0217

M3 - Journal article

VL - 15

SP - 3257

EP - 3265

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 7

ER -