کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10798152 | 1053300 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of the ion transport activity of the budding yeast Na+/H+ antiporter, Nha1p, using isolated secretory vesicles
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کلمات کلیدی
ORFeGFPPMFCCCPAcmANHESDS PAGE9-amino-6-chloro-2-methoxyacridine - 9-آمینو-6-کلرو-2-متکی آکرییدینNa+/H+ exchanger - Na + / H + مبدلnHA - NHASDS polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمید SDSElectrogenicity - الکترونی بودنIon selectivity - انتخاب یونNa+/H+ antiporter - ضد عفونی کننده Na + / H +open reading frame - قاب خواندن بازproton motive force - نیروی حرکتی پروتونenhanced green fluorescent protein - پروتئین فلورسنت سبز افزایش یافته استcarbonyl cyanide m-chlorophenylhydrazone - کربنیل سیانید m-chlorophenylhydrazone
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of the ion transport activity of the budding yeast Na+/H+ antiporter, Nha1p, using isolated secretory vesicles Characterization of the ion transport activity of the budding yeast Na+/H+ antiporter, Nha1p, using isolated secretory vesicles](/preview/png/10798152.png)
چکیده انگلیسی
The Saccharomyces cerevisiae Nha1p, a plasma membrane protein belonging to the monovalent cation/proton antiporter family, plays a key role in the salt tolerance and pH regulation of cells. We examined the molecular function of Nha1p by using secretory vesicles isolated from a temperature sensitive secretory mutant, sec4-2, in vitro. The isolated secretory vesicles contained newly synthesized Nha1p en route to the plasma membrane and showed antiporter activity exchanging H+ for monovalent alkali metal cations. An amino acid substitution in Nha1p (D266N, Asp-266 to Asn) almost completely abolished the Na+/H+ but not K+/H+ antiport activity, confirming the validity of this assay system as well as the functional importance of Asp-266, especially for selectivity of substrate cations. Nha1p catalyzes transport of Na+ and K+ with similar affinity (12.7 mM and 12.4 mM), and with lower affinity for Rb+ and Li+. Nha1p activity is associated with a net charge movement across the membrane, transporting more protons per single sodium ion (i.e., electrogenic). This feature is similar to the bacterial Na+/H+ antiporters, whereas other known eukaryotic Na+/H+ antiporters are electroneutral. The ion selectivity and the stoichiometry suggest a unique physiological role of Nha1p which is distinct from that of other known Na+/H+ antiporters.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1712, Issue 2, 1 July 2005, Pages 185-196
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1712, Issue 2, 1 July 2005, Pages 185-196
نویسندگان
Ryuichi Ohgaki, Norihiro Nakamura, Keiji Mitsui, Hiroshi Kanazawa,