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Characterization of a novel tyrosine permease of lager brewing yeast shared by Saccharomyces cerevisiae strain RM11-1a.
FEMS Yeast Res. 2007 Dec; 7(8):1350-61.FY

Abstract

In Saccharomyces cerevisiae yeast, the uptake of aromatic amino acids is mediated by the relatively specific permeases Tat1p, Tat2p, Bap2p, and Bap3p, as well as by two other permeases with broader specificities: Gap1p and Agp1p. Here, a novel permease gene TAT3 (Tyrosine Amino acid Transporter) identified in the S. cerevisiae-type subset genome of the lager brewing yeast strain Weihenstephan Nr.34 (34/70) is reported. The TAT3 sequence was also found in the genome of S. cerevisiae strain RM11-1a, but not in S. cerevisiae strain S288C. Tat3p showed a significant similarity to Penicillium chrysogenum ArlP permease, which has transport activity for aromatic amino acids and leucine. When overexpressed in ssy1Delta gap1Delta mutant cells, Tat3p exhibited a tyrosine transport activity with an apparent K(m) of 160 microM. TAT3 transcription in lager brewing yeast was subjected to nitrogen catabolite repression in a manner similar to that of GAP1. Furthermore, the subcellular localization of Tat3p-green fluorescent protein (GFP) fusion protein was dependent on the quality of the nitrogen source, indicating a post-translational control of Tat3p function.

Links

Publisher Full Text
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onlinelibrary.wiley.com
onlinelibrary.wiley.com

Authors+Show Affiliations

Omura F
Suntory Research Center, Shimamoto-cho, Mishima-gun, Osaka, Japan. fumihiko_omura@suntory.co.jp
Hatanaka H
No affiliation info available
Nakao Y
No affiliation info available

MeSH

Amino Acid SequenceAmino Acid Transport SystemsDNA, FungalGene Expression Regulation, FungalGenetic Complementation TestMolecular Sequence DataPenicillium chrysogenumPhylogenySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Analysis, DNASequence Homology, Amino AcidTyrosine

Pub Type(s)

Journal Article

Language

eng

PubMed ID

17825063

Citation

Omura, Fumihiko, et al. "Characterization of a Novel Tyrosine Permease of Lager Brewing Yeast Shared By Saccharomyces Cerevisiae Strain RM11-1a." FEMS Yeast Research, vol. 7, no. 8, 2007, pp. 1350-61.
Omura F, Hatanaka H, Nakao Y. Characterization of a novel tyrosine permease of lager brewing yeast shared by Saccharomyces cerevisiae strain RM11-1a. FEMS Yeast Res. 2007;7(8):1350-61.
Omura, F., Hatanaka, H., & Nakao, Y. (2007). Characterization of a novel tyrosine permease of lager brewing yeast shared by Saccharomyces cerevisiae strain RM11-1a. FEMS Yeast Research, 7(8), 1350-61.
Omura F, Hatanaka H, Nakao Y. Characterization of a Novel Tyrosine Permease of Lager Brewing Yeast Shared By Saccharomyces Cerevisiae Strain RM11-1a. FEMS Yeast Res. 2007;7(8):1350-61. PubMed PMID: 17825063.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of a novel tyrosine permease of lager brewing yeast shared by Saccharomyces cerevisiae strain RM11-1a. AU - Omura,Fumihiko, AU - Hatanaka,Haruyo, AU - Nakao,Yoshihiro, Y1 - 2007/09/06/ PY - 2007/9/11/pubmed PY - 2008/1/4/medline PY - 2007/9/11/entrez SP - 1350 EP - 61 JF - FEMS yeast research JO - FEMS Yeast Res VL - 7 IS - 8 N2 - In Saccharomyces cerevisiae yeast, the uptake of aromatic amino acids is mediated by the relatively specific permeases Tat1p, Tat2p, Bap2p, and Bap3p, as well as by two other permeases with broader specificities: Gap1p and Agp1p. Here, a novel permease gene TAT3 (Tyrosine Amino acid Transporter) identified in the S. cerevisiae-type subset genome of the lager brewing yeast strain Weihenstephan Nr.34 (34/70) is reported. The TAT3 sequence was also found in the genome of S. cerevisiae strain RM11-1a, but not in S. cerevisiae strain S288C. Tat3p showed a significant similarity to Penicillium chrysogenum ArlP permease, which has transport activity for aromatic amino acids and leucine. When overexpressed in ssy1Delta gap1Delta mutant cells, Tat3p exhibited a tyrosine transport activity with an apparent K(m) of 160 microM. TAT3 transcription in lager brewing yeast was subjected to nitrogen catabolite repression in a manner similar to that of GAP1. Furthermore, the subcellular localization of Tat3p-green fluorescent protein (GFP) fusion protein was dependent on the quality of the nitrogen source, indicating a post-translational control of Tat3p function. SN - 1567-1356 UR - https://www.unboundmedicine.com/medline/citation/17825063/Characterization_of_a_novel_tyrosine_permease_of_lager_brewing_yeast_shared_by_Saccharomyces_cerevisiae_strain_RM11_1a_ L2 - https://academic.oup.com/femsyr/article-lookup/doi/10.1111/j.1567-1364.2007.00310.x DB - PRIME DP - Unbound Medicine ER -