Cargando…

The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity

Multidrug and toxic compound extrusion (MATE) transporters in eukaryotes have been characterized to be antiporters that mediate the transport of substrates in exchange for protons. In plants, alkaloids, phytohormones, ion chelators, and flavonoids have been reported to be the substrates of MATE tran...

Descripción completa

Detalles Bibliográficos
Autores principales: Ku, Yee-Shan, Cheng, Sau-Shan, Cheung, Ming-Yan, Niu, Yongchao, Liu, Ailin, Chung, Gyuhwa, Lam, Hon-Ming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880658/
https://www.ncbi.nlm.nih.gov/pubmed/35207127
http://dx.doi.org/10.3390/membranes12020206
_version_ 1784659269369462784
author Ku, Yee-Shan
Cheng, Sau-Shan
Cheung, Ming-Yan
Niu, Yongchao
Liu, Ailin
Chung, Gyuhwa
Lam, Hon-Ming
author_facet Ku, Yee-Shan
Cheng, Sau-Shan
Cheung, Ming-Yan
Niu, Yongchao
Liu, Ailin
Chung, Gyuhwa
Lam, Hon-Ming
author_sort Ku, Yee-Shan
collection PubMed
description Multidrug and toxic compound extrusion (MATE) transporters in eukaryotes have been characterized to be antiporters that mediate the transport of substrates in exchange for protons. In plants, alkaloids, phytohormones, ion chelators, and flavonoids have been reported to be the substrates of MATE transporters. Structural analyses have been conducted to dissect the functional significance of various motifs of MATE proteins. However, an understanding of the functions of the N- and C-termini has been inadequate. Here, by performing phylogenetic analyses and protein sequence alignment of 14 representative plant species, we identified a distinctive N-terminal poly-glutamate motif among a cluster of MATE proteins in soybean. Amongst them, GmMATE4 has the most consecutive glutamate residues at the N-terminus. A subcellular localization study showed that GmMATE4 was localized at the vacuolar membrane-like structure. Protein charge prediction showed that the mutation of the glutamate residues to alanine would reduce the negative charge at the N-terminus. Using yeast as the model, we showed that GmMATE4 mediated the transport of daidzein, genistein, glycitein, and glycitin. In addition, the glutamate-to-alanine mutation reduced the isoflavone transport capacity of GmMATE4. Altogether, we demonstrated GmMATE4 as an isoflavone transporter and the functional significance of the N-terminal poly-glutamate motif of GmMATE4 for regulating the isoflavone transport activity.
format Online
Article
Text
id pubmed-8880658
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-88806582022-02-26 The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity Ku, Yee-Shan Cheng, Sau-Shan Cheung, Ming-Yan Niu, Yongchao Liu, Ailin Chung, Gyuhwa Lam, Hon-Ming Membranes (Basel) Article Multidrug and toxic compound extrusion (MATE) transporters in eukaryotes have been characterized to be antiporters that mediate the transport of substrates in exchange for protons. In plants, alkaloids, phytohormones, ion chelators, and flavonoids have been reported to be the substrates of MATE transporters. Structural analyses have been conducted to dissect the functional significance of various motifs of MATE proteins. However, an understanding of the functions of the N- and C-termini has been inadequate. Here, by performing phylogenetic analyses and protein sequence alignment of 14 representative plant species, we identified a distinctive N-terminal poly-glutamate motif among a cluster of MATE proteins in soybean. Amongst them, GmMATE4 has the most consecutive glutamate residues at the N-terminus. A subcellular localization study showed that GmMATE4 was localized at the vacuolar membrane-like structure. Protein charge prediction showed that the mutation of the glutamate residues to alanine would reduce the negative charge at the N-terminus. Using yeast as the model, we showed that GmMATE4 mediated the transport of daidzein, genistein, glycitein, and glycitin. In addition, the glutamate-to-alanine mutation reduced the isoflavone transport capacity of GmMATE4. Altogether, we demonstrated GmMATE4 as an isoflavone transporter and the functional significance of the N-terminal poly-glutamate motif of GmMATE4 for regulating the isoflavone transport activity. MDPI 2022-02-10 /pmc/articles/PMC8880658/ /pubmed/35207127 http://dx.doi.org/10.3390/membranes12020206 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ku, Yee-Shan
Cheng, Sau-Shan
Cheung, Ming-Yan
Niu, Yongchao
Liu, Ailin
Chung, Gyuhwa
Lam, Hon-Ming
The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title_full The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title_fullStr The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title_full_unstemmed The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title_short The Poly-Glutamate Motif of GmMATE4 Regulates Its Isoflavone Transport Activity
title_sort poly-glutamate motif of gmmate4 regulates its isoflavone transport activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880658/
https://www.ncbi.nlm.nih.gov/pubmed/35207127
http://dx.doi.org/10.3390/membranes12020206
work_keys_str_mv AT kuyeeshan thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT chengsaushan thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT cheungmingyan thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT niuyongchao thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT liuailin thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT chunggyuhwa thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT lamhonming thepolyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT kuyeeshan polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT chengsaushan polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT cheungmingyan polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT niuyongchao polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT liuailin polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT chunggyuhwa polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity
AT lamhonming polyglutamatemotifofgmmate4regulatesitsisoflavonetransportactivity