The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum

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The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum. / Neve, S; Tornehave, D; Corydon, T J; Kristiansen, K.

In: Cell Biology International, Vol. 23, No. 11, 1999, p. 719-28.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Neve, S, Tornehave, D, Corydon, TJ & Kristiansen, K 1999, 'The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum', Cell Biology International, vol. 23, no. 11, pp. 719-28. https://doi.org/10.1006/cbir.1998.0336

APA

Neve, S., Tornehave, D., Corydon, T. J., & Kristiansen, K. (1999). The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum. Cell Biology International, 23(11), 719-28. https://doi.org/10.1006/cbir.1998.0336

Vancouver

Neve S, Tornehave D, Corydon TJ, Kristiansen K. The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum. Cell Biology International. 1999;23(11):719-28. https://doi.org/10.1006/cbir.1998.0336

Author

Neve, S ; Tornehave, D ; Corydon, T J ; Kristiansen, K. / The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum. In: Cell Biology International. 1999 ; Vol. 23, No. 11. pp. 719-28.

Bibtex

@article{f56003900fae11de8478000ea68e967b,
title = "The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum",
abstract = "The expression and intracellular localization of the Tetrahymena homolog of 4-hydroxyphenylpyruvate dioxygenase (HPPD) were investigated in wild-type Tetrahymena thermophila strain B1868 VII and the mutant strains IIG8, defective in food vacuole formation, MS-1, blocked in secretion of lysosomal enzymes, and SB 281, defective in mucocyst maturation. Immunoelectron microscopy and confocal laser scanning microscopy demonstrated that Tetrahymena HPPD primarily localized to membranes of the endoplasmic reticulum. In addition, Tetrahymena HPPD was detected in association with membranes of the Golgi apparatus, and transport vesicles in exponentially growing wild-type and mutant strains. In starved cells, Tetrahymena HPPD localized exclusively to membranes of small vesicles. Since no de novo synthesis of Tetrahymena HPPD takes place in cells starved for more than 30 min, these results suggest that there is a flow of Tetrahymena HPPD from the endoplasmic reticulum to small vesicles, possibly via the Golgi apparatus, and that Tetrahymena HPPD contains a signal for vesicle membrane retrieval or retention.",
author = "S Neve and D Tornehave and Corydon, {T J} and K Kristiansen",
note = "Keywords: 4-Hydroxyphenylpyruvate Dioxygenase; Animals; Bacteria; Endoplasmic Reticulum; Intracellular Membranes; Mammals; Recombinant Fusion Proteins; Tetrahymena thermophila; Vacuoles",
year = "1999",
doi = "10.1006/cbir.1998.0336",
language = "English",
volume = "23",
pages = "719--28",
journal = "Cell Biology International",
issn = "1065-6995",
publisher = "Academic Press",
number = "11",

}

RIS

TY - JOUR

T1 - The Tetrahymena homolog of bacterial and mammalian 4-hydroxyphenylpyruvate dioxygenases localizes to membranes of the endoplasmic reticulum

AU - Neve, S

AU - Tornehave, D

AU - Corydon, T J

AU - Kristiansen, K

N1 - Keywords: 4-Hydroxyphenylpyruvate Dioxygenase; Animals; Bacteria; Endoplasmic Reticulum; Intracellular Membranes; Mammals; Recombinant Fusion Proteins; Tetrahymena thermophila; Vacuoles

PY - 1999

Y1 - 1999

N2 - The expression and intracellular localization of the Tetrahymena homolog of 4-hydroxyphenylpyruvate dioxygenase (HPPD) were investigated in wild-type Tetrahymena thermophila strain B1868 VII and the mutant strains IIG8, defective in food vacuole formation, MS-1, blocked in secretion of lysosomal enzymes, and SB 281, defective in mucocyst maturation. Immunoelectron microscopy and confocal laser scanning microscopy demonstrated that Tetrahymena HPPD primarily localized to membranes of the endoplasmic reticulum. In addition, Tetrahymena HPPD was detected in association with membranes of the Golgi apparatus, and transport vesicles in exponentially growing wild-type and mutant strains. In starved cells, Tetrahymena HPPD localized exclusively to membranes of small vesicles. Since no de novo synthesis of Tetrahymena HPPD takes place in cells starved for more than 30 min, these results suggest that there is a flow of Tetrahymena HPPD from the endoplasmic reticulum to small vesicles, possibly via the Golgi apparatus, and that Tetrahymena HPPD contains a signal for vesicle membrane retrieval or retention.

AB - The expression and intracellular localization of the Tetrahymena homolog of 4-hydroxyphenylpyruvate dioxygenase (HPPD) were investigated in wild-type Tetrahymena thermophila strain B1868 VII and the mutant strains IIG8, defective in food vacuole formation, MS-1, blocked in secretion of lysosomal enzymes, and SB 281, defective in mucocyst maturation. Immunoelectron microscopy and confocal laser scanning microscopy demonstrated that Tetrahymena HPPD primarily localized to membranes of the endoplasmic reticulum. In addition, Tetrahymena HPPD was detected in association with membranes of the Golgi apparatus, and transport vesicles in exponentially growing wild-type and mutant strains. In starved cells, Tetrahymena HPPD localized exclusively to membranes of small vesicles. Since no de novo synthesis of Tetrahymena HPPD takes place in cells starved for more than 30 min, these results suggest that there is a flow of Tetrahymena HPPD from the endoplasmic reticulum to small vesicles, possibly via the Golgi apparatus, and that Tetrahymena HPPD contains a signal for vesicle membrane retrieval or retention.

U2 - 10.1006/cbir.1998.0336

DO - 10.1006/cbir.1998.0336

M3 - Journal article

C2 - 10736196

VL - 23

SP - 719

EP - 728

JO - Cell Biology International

JF - Cell Biology International

SN - 1065-6995

IS - 11

ER -

ID: 11254171