Involvement of histidine-rich domain of ZIP family transporter TjZNT1 in metal ion specificity

The Zrt/Irt-like protein (ZIP) family generally contributes to metal homeostasis by regulating cation transport into the cytoplasm. Most ZIP members have a long variable loop between transmembrane domains III and IV, and these loops are predicted to be located in the cytoplasm. The loops contain a h...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 46(2008), 5-6 vom: 15. Mai, Seite 601-6
1. Verfasser: Nishida, Sho (VerfasserIn)
Weitere Verfasser: Mizuno, Takafumi, Obata, Hitoshi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Cation Transport Proteins Membrane Transport Proteins Metals Recombinant Fusion Proteins Cadmium 00BH33GNGH Green Fluorescent Proteins 147336-22-9 mehr... Zinc J41CSQ7QDS
LEADER 01000naa a22002652 4500
001 NLM179134779
003 DE-627
005 20231223153251.0
007 cr uuu---uuuuu
008 231223s2008 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.plaphy.2008.02.011  |2 doi 
028 5 2 |a pubmed24n0597.xml 
035 |a (DE-627)NLM179134779 
035 |a (NLM)18434175 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Nishida, Sho  |e verfasserin  |4 aut 
245 1 0 |a Involvement of histidine-rich domain of ZIP family transporter TjZNT1 in metal ion specificity 
264 1 |c 2008 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 23.09.2008 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a The Zrt/Irt-like protein (ZIP) family generally contributes to metal homeostasis by regulating cation transport into the cytoplasm. Most ZIP members have a long variable loop between transmembrane domains III and IV, and these loops are predicted to be located in the cytoplasm. The loops contain a histidine-rich domain (HRD) postulated to serve as a metal ion binding site; however, its role has not yet been determined. We previously determined that deletion of the HRD did not affect the Ni tolerance ability of TjZNT1-a ZIP transporter that confers high Ni tolerance to yeast. In this study, we investigated the effect of HRD deletion on the ion transport ability of TjZNT1. The deletion of HRD increased the specificity for Zn2+, but not for Cd2+. In addition, we confirmed subcellular localizations of TjZNT1 and HRD-deleted mutants by green fluorescence protein (GFP)-fused proteins, indicating that the deletion of HRD did not affect the localization of TjZNT1. From these results, we propose that the HRD could be involved in the ion specificity of TjZNT1 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Cation Transport Proteins  |2 NLM 
650 7 |a Membrane Transport Proteins  |2 NLM 
650 7 |a Metals  |2 NLM 
650 7 |a Recombinant Fusion Proteins  |2 NLM 
650 7 |a Cadmium  |2 NLM 
650 7 |a 00BH33GNGH  |2 NLM 
650 7 |a Green Fluorescent Proteins  |2 NLM 
650 7 |a 147336-22-9  |2 NLM 
650 7 |a Zinc  |2 NLM 
650 7 |a J41CSQ7QDS  |2 NLM 
700 1 |a Mizuno, Takafumi  |e verfasserin  |4 aut 
700 1 |a Obata, Hitoshi  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 46(2008), 5-6 vom: 15. Mai, Seite 601-6  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:46  |g year:2008  |g number:5-6  |g day:15  |g month:05  |g pages:601-6 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2008.02.011  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 46  |j 2008  |e 5-6  |b 15  |c 05  |h 601-6