Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport

Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within trans...
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Autor*in:	Sun, Ye [verfasserIn] Ward, John M

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2012

Schlagwörter:	Sucrose transporter Major facilitator superfamily Substrate binding Mutagenesis

Anmerkung:	© Sun and Ward; licensee BioMed Central Ltd. 2012

Übergeordnetes Werk:	Enthalten in: BMC biochemistry - London : BioMed Central, 2000, 13(2012), 1 vom: 21. Nov.
Übergeordnetes Werk:	volume:13 ; year:2012 ; number:1 ; day:21 ; month:11

Links:	Volltext

DOI / URN:	10.1186/1471-2091-13-26

Katalog-ID:	SPR026817780

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245	1	0	\|a Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
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520			\|a Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation.
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Indexfelder

author_variant	y s ys j m w jm jmw
matchkey_str	article:14712091:2012----::r18nieurstasotrsu1srcafr
hierarchy_sort_str	2012
publishDate	2012
allfields	10.1186/1471-2091-13-26 doi (DE-627)SPR026817780 (SPR)1471-2091-13-26-e DE-627 ger DE-627 rakwb eng Sun, Ye verfasserin aut Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sun and Ward; licensee BioMed Central Ltd. 2012 Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213 Ward, John M aut Enthalten in BMC biochemistry London : BioMed Central, 2000 13(2012), 1 vom: 21. Nov. (DE-627)326179399 (DE-600)2041216-2 1471-2091 nnns volume:13 year:2012 number:1 day:21 month:11 https://dx.doi.org/10.1186/1471-2091-13-26 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2012 1 21 11
spelling	10.1186/1471-2091-13-26 doi (DE-627)SPR026817780 (SPR)1471-2091-13-26-e DE-627 ger DE-627 rakwb eng Sun, Ye verfasserin aut Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sun and Ward; licensee BioMed Central Ltd. 2012 Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213 Ward, John M aut Enthalten in BMC biochemistry London : BioMed Central, 2000 13(2012), 1 vom: 21. Nov. (DE-627)326179399 (DE-600)2041216-2 1471-2091 nnns volume:13 year:2012 number:1 day:21 month:11 https://dx.doi.org/10.1186/1471-2091-13-26 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2012 1 21 11
allfields_unstemmed	10.1186/1471-2091-13-26 doi (DE-627)SPR026817780 (SPR)1471-2091-13-26-e DE-627 ger DE-627 rakwb eng Sun, Ye verfasserin aut Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sun and Ward; licensee BioMed Central Ltd. 2012 Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213 Ward, John M aut Enthalten in BMC biochemistry London : BioMed Central, 2000 13(2012), 1 vom: 21. Nov. (DE-627)326179399 (DE-600)2041216-2 1471-2091 nnns volume:13 year:2012 number:1 day:21 month:11 https://dx.doi.org/10.1186/1471-2091-13-26 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2012 1 21 11
allfieldsGer	10.1186/1471-2091-13-26 doi (DE-627)SPR026817780 (SPR)1471-2091-13-26-e DE-627 ger DE-627 rakwb eng Sun, Ye verfasserin aut Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sun and Ward; licensee BioMed Central Ltd. 2012 Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213 Ward, John M aut Enthalten in BMC biochemistry London : BioMed Central, 2000 13(2012), 1 vom: 21. Nov. (DE-627)326179399 (DE-600)2041216-2 1471-2091 nnns volume:13 year:2012 number:1 day:21 month:11 https://dx.doi.org/10.1186/1471-2091-13-26 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2012 1 21 11
allfieldsSound	10.1186/1471-2091-13-26 doi (DE-627)SPR026817780 (SPR)1471-2091-13-26-e DE-627 ger DE-627 rakwb eng Sun, Ye verfasserin aut Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Sun and Ward; licensee BioMed Central Ltd. 2012 Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213 Ward, John M aut Enthalten in BMC biochemistry London : BioMed Central, 2000 13(2012), 1 vom: 21. Nov. (DE-627)326179399 (DE-600)2041216-2 1471-2091 nnns volume:13 year:2012 number:1 day:21 month:11 https://dx.doi.org/10.1186/1471-2091-13-26 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2012 1 21 11
language	English
source	Enthalten in BMC biochemistry 13(2012), 1 vom: 21. Nov. volume:13 year:2012 number:1 day:21 month:11
sourceStr	Enthalten in BMC biochemistry 13(2012), 1 vom: 21. Nov. volume:13 year:2012 number:1 day:21 month:11
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Sucrose transporter Major facilitator superfamily Substrate binding Mutagenesis
isfreeaccess_bool	true
container_title	BMC biochemistry
authorswithroles_txt_mv	Sun, Ye @@aut@@ Ward, John M @@aut@@
publishDateDaySort_date	2012-11-21T00:00:00Z
hierarchy_top_id	326179399
id	SPR026817780
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SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. 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author	Sun, Ye
spellingShingle	Sun, Ye misc Sucrose transporter misc Major facilitator superfamily misc Substrate binding misc Mutagenesis Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
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topic_title	Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport Sucrose transporter (dpeaa)DE-He213 Major facilitator superfamily (dpeaa)DE-He213 Substrate binding (dpeaa)DE-He213 Mutagenesis (dpeaa)DE-He213
topic	misc Sucrose transporter misc Major facilitator superfamily misc Substrate binding misc Mutagenesis
topic_unstemmed	misc Sucrose transporter misc Major facilitator superfamily misc Substrate binding misc Mutagenesis
topic_browse	misc Sucrose transporter misc Major facilitator superfamily misc Substrate binding misc Mutagenesis
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
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title_full	Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
author_sort	Sun, Ye
journal	BMC biochemistry
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author_browse	Sun, Ye Ward, John M
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author-letter	Sun, Ye
doi_str_mv	10.1186/1471-2091-13-26
title_sort	arg188 in rice sucrose transporter ossut1 is crucial for substrate transport
title_auth	Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
abstract	Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. © Sun and Ward; licensee BioMed Central Ltd. 2012
abstractGer	Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. © Sun and Ward; licensee BioMed Central Ltd. 2012
abstract_unstemmed	Background Plant sucrose uptake transporters (SUTs) are $ H^{+} $/sucrose symporters related to the major facilitator superfamily (MFS). SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. We propose that R188 interacts with glucosyl 3-OH and 4-OH during translocation. © Sun and Ward; licensee BioMed Central Ltd. 2012
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title_short	Arg188 in rice sucrose transporter OsSUT1 is crucial for substrate transport
url	https://dx.doi.org/10.1186/1471-2091-13-26
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author2	Ward, John M
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up_date	2024-07-03T22:53:57.341Z
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SUTs are essential for plant growth but little is known about their transport mechanism. Recent work identified several conserved, charged amino acids within transmembrane spans (TMS) in SUTs that are essential for transport activity. Here we further evaluated the role of one of these positions, R188 in the fourth TMS of OsSUT1, a type II SUT. Results The OsSUT1(R188K) mutant, studied by expression in plants, yeast, and Xenopus oocytes, did not transport sucrose but showed a $ H^{+} $ leak that was blocked by sucrose. The $ H^{+} $ leak was also blocked by β-phenyl glucoside which is not translocated by OsSUT1. Replacing the corresponding Arg in type I and type III SUTs, AtSUC1(R163K) and LjSUT4(R169K), respectively, also resulted in loss of sucrose transport activity. Fluorination at the glucosyl 3 and 4 positions of α-phenyl glucoside greatly decreased transport by wild type OsSUT1 but did not affect the ability to block $ H^{+} $ leak in the R188K mutant. Conclusion OsSUT1 R188 appears to be essential for sucrose translocation but not for substrate interaction that blocks $ H^{+} $ leak. Therefore, we propose that an additional binding site functions in the initial recognition of substrates. The corresponding Arg in type I and III SUTs are equally important. 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