Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases. / Düring-Olsen, Louis; Regenberg, Birgitte; Gjermansen, Claes; Kielland-Brandt, Morten C.; Hansen, Jørgen.

In: Current Genetics, Vol. 35, No. 6, 15.08.1999, p. 609-617.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Düring-Olsen, L, Regenberg, B, Gjermansen, C, Kielland-Brandt, MC & Hansen, J 1999, 'Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases', Current Genetics, vol. 35, no. 6, pp. 609-617. https://doi.org/10.1007/s002940050459

APA

Düring-Olsen, L., Regenberg, B., Gjermansen, C., Kielland-Brandt, M. C., & Hansen, J. (1999). Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases. Current Genetics, 35(6), 609-617. https://doi.org/10.1007/s002940050459

Vancouver

Düring-Olsen L, Regenberg B, Gjermansen C, Kielland-Brandt MC, Hansen J. Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases. Current Genetics. 1999 Aug 15;35(6):609-617. https://doi.org/10.1007/s002940050459

Author

Düring-Olsen, Louis ; Regenberg, Birgitte ; Gjermansen, Claes ; Kielland-Brandt, Morten C. ; Hansen, Jørgen. / Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases. In: Current Genetics. 1999 ; Vol. 35, No. 6. pp. 609-617.

Bibtex

@article{c1e6a139a46a436490e701dbd4f001f4,
title = "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases",
abstract = "Uptake by Saccharomyces cerevisiae of the sulphur-containing amino acid L-cysteine was found to be non-saturable under various conditions, and uptake kinetics suggested the existence of two or more transport systems in addition to the general amino-acid permease, Gap1p. Overexpression studies identified BAP2, BAP3, AGP1 and GNP1 as genes encoding transporters of cysteine. Uptake studies with disruption mutants confirmed this. and identified two additional genes for transporters of cysteine, TAT1 and TAT2, both very homologous to BAP2, BAP3, AGP1 and GNP1. While Gap 1p and Agp 1p appear to be the main cysteine transporters on the non-repressing nitrogen source proline, Bap2p, Bap3p, Tat1p, Tat2p, Agp1p and Gnp1p are all important for cysteine uptake on ammonium-based medium. Furthermore, whereas Bap2p, Bap3p, Tat1p and Tat2p seem most important under amino acid-rich conditions, Agp 1p contributes significantly when only ammonium is present, and Gnp1p only contributes under the latter condition.",
keywords = "Amino-acid permeases, Cysteine uptake, Saccharomyces cerevisiae",
author = "Louis D{\"u}ring-Olsen and Birgitte Regenberg and Claes Gjermansen and Kielland-Brandt, {Morten C.} and J{\o}rgen Hansen",
year = "1999",
month = aug,
day = "15",
doi = "10.1007/s002940050459",
language = "English",
volume = "35",
pages = "609--617",
journal = "Current Genetics",
issn = "0172-8083",
publisher = "Springer",
number = "6",

}

RIS

TY - JOUR

T1 - Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases

AU - Düring-Olsen, Louis

AU - Regenberg, Birgitte

AU - Gjermansen, Claes

AU - Kielland-Brandt, Morten C.

AU - Hansen, Jørgen

PY - 1999/8/15

Y1 - 1999/8/15

N2 - Uptake by Saccharomyces cerevisiae of the sulphur-containing amino acid L-cysteine was found to be non-saturable under various conditions, and uptake kinetics suggested the existence of two or more transport systems in addition to the general amino-acid permease, Gap1p. Overexpression studies identified BAP2, BAP3, AGP1 and GNP1 as genes encoding transporters of cysteine. Uptake studies with disruption mutants confirmed this. and identified two additional genes for transporters of cysteine, TAT1 and TAT2, both very homologous to BAP2, BAP3, AGP1 and GNP1. While Gap 1p and Agp 1p appear to be the main cysteine transporters on the non-repressing nitrogen source proline, Bap2p, Bap3p, Tat1p, Tat2p, Agp1p and Gnp1p are all important for cysteine uptake on ammonium-based medium. Furthermore, whereas Bap2p, Bap3p, Tat1p and Tat2p seem most important under amino acid-rich conditions, Agp 1p contributes significantly when only ammonium is present, and Gnp1p only contributes under the latter condition.

AB - Uptake by Saccharomyces cerevisiae of the sulphur-containing amino acid L-cysteine was found to be non-saturable under various conditions, and uptake kinetics suggested the existence of two or more transport systems in addition to the general amino-acid permease, Gap1p. Overexpression studies identified BAP2, BAP3, AGP1 and GNP1 as genes encoding transporters of cysteine. Uptake studies with disruption mutants confirmed this. and identified two additional genes for transporters of cysteine, TAT1 and TAT2, both very homologous to BAP2, BAP3, AGP1 and GNP1. While Gap 1p and Agp 1p appear to be the main cysteine transporters on the non-repressing nitrogen source proline, Bap2p, Bap3p, Tat1p, Tat2p, Agp1p and Gnp1p are all important for cysteine uptake on ammonium-based medium. Furthermore, whereas Bap2p, Bap3p, Tat1p and Tat2p seem most important under amino acid-rich conditions, Agp 1p contributes significantly when only ammonium is present, and Gnp1p only contributes under the latter condition.

KW - Amino-acid permeases

KW - Cysteine uptake

KW - Saccharomyces cerevisiae

UR - http://www.scopus.com/inward/record.url?scp=0032801817&partnerID=8YFLogxK

U2 - 10.1007/s002940050459

DO - 10.1007/s002940050459

M3 - Journal article

C2 - 10467005

AN - SCOPUS:0032801817

VL - 35

SP - 609

EP - 617

JO - Current Genetics

JF - Current Genetics

SN - 0172-8083

IS - 6

ER -

ID: 239906267