2010
DOI: 10.1021/bi100239j
|View full text |Cite
|
Sign up to set email alerts
|

Functionally Important Amino Acids in the Arabidopsis Thylakoid Phosphate Transporter: Homology Modeling and Site-Directed Mutagenesis

Abstract: The anion transporter 1 (ANTR1) from Arabidopsis thaliana, homologous to the mammalian members of the solute carrier 17 (SLC17) family, is located in the chloroplast thylakoid membrane. When expressed heterologously in Escherichia coli, ANTR1 mediates a Na+-dependent active transport of inorganic phosphate (Pi). The aim of this study was to identify amino acid residues involved in Pi binding and translocation by ANTR1 and in the Na+ dependence of its activity. A three-dimensional structural model of ANTR1 was … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
10
0

Year Published

2012
2012
2018
2018

Publication Types

Select...
7
1

Relationship

5
3

Authors

Journals

citations
Cited by 14 publications
(11 citation statements)
references
References 43 publications
0
10
0
Order By: Relevance
“…PHT4;1 belongs to the PHT4 family of Pi symporters and was localized to the thylakoid membrane and to the chloroplast envelope (Pavon et al 2008, Ferro et al 2010. Yeast complementation experiments revealed a H + -dependent mechanism of Pi transport (Guo et al 2008), however, assays in E. coli indicated PHT4;1 as a high-affinity Na + -dependent Pi transporter (Pavon et al 2008, Ruiz-Pavon et al 2010. More recently, the envelope PHT4;4 transporter was found to preferentially function in ascorbate rather than Pi transport based on uptake assays in proteoliposomes (Miyaji et al 2015).…”
Section: Ion Transportersmentioning
confidence: 99%
“…PHT4;1 belongs to the PHT4 family of Pi symporters and was localized to the thylakoid membrane and to the chloroplast envelope (Pavon et al 2008, Ferro et al 2010. Yeast complementation experiments revealed a H + -dependent mechanism of Pi transport (Guo et al 2008), however, assays in E. coli indicated PHT4;1 as a high-affinity Na + -dependent Pi transporter (Pavon et al 2008, Ruiz-Pavon et al 2010. More recently, the envelope PHT4;4 transporter was found to preferentially function in ascorbate rather than Pi transport based on uptake assays in proteoliposomes (Miyaji et al 2015).…”
Section: Ion Transportersmentioning
confidence: 99%
“…Channels/porins  K + channel (SynK) Synechocystis slr0498 K + Photosynthesis: regulation of the electric component of proton motive force[46, 51] Two-pore K + channel 3 (TPK3) Arabidopsis At4g18160 K + ?Not determined[46, 47, 128] Chloride channel e (CLCe) Arabidopsis At4g35440 Cl − , NO 2 − Photosynthesis, nitrate homeostasis[57, 58] Tonoplast intrinsic protein 2;1 (TIP2;1) Arabidopsis At3g16240 H 2 O, H 2 O 2 , NH 3 , ureaNot determined[34, 35, 61] TC #2. Secondary transporters  Phosphate transporter 4;1 (PHT4;1) Arabidopsis At2g29650 PiPSII repair and photoprotection[66, 67, 71] Thylakoid ATP/ADP carrier (TAAC) Arabidopsis At5g01500 ATP, ADP, PAPS, PAPThylakoid biogenesis, PSII repair and photoprotection, sulfur metabolism, retrograde signaling[78, 79, 82, 84] Na + /H + antiporter NhaS3 Synechocystis sll0689 Na + , H + Essential gene. Balance of Na + /K + ratio.…”
Section: The Photosynthetic Machinery Requires Thylakoid Channels Andmentioning
confidence: 99%
“…() observed H + ‐dependent Pi transport when it was expressed in Saccharomyces cerevisiae . Several residues that are important for Pi transport and its Na + dependence were identified using homology modeling, site‐directed mutagenesis and functional characterization in Escherichia coli (Ruiz‐Pavon et al ., ). It was suggested that the direction of transport across thylakoids depends on the electrochemical gradient of Pi, and that H + , Na + or K + ion gradients could drive the transport (Guo et al ., ; Pavon et al ., ).…”
Section: Introductionmentioning
confidence: 97%