کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5507134 | 1400312 | 2017 | 34 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Electrostatic interaction of positive charges on the surface of Psb31 with photosystem II in the diatom Chaetoceros gracilis
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کلمات کلیدی
ChlNSPGMEGlycine methyl ester2-(N-morpholino)ethanesulfonic acid - 2- (N-مورفولینو) اتان سولفونیک اسیدdiatom - دیاتومChlorophyll - سبزینه یا کلروفیلPhotosystem - سیستم عکسMatrix-assisted laser desorption ionization time-of-flight mass spectrometry - طیف سنجی جرمی یونیزاسیون یونیزاسیون لیزر جذب ماتریسPhotosystem II - فتوسیستم 2MALDI-TOF MS - مالدی توف MSMeS - مسExtrinsic proteins - پروتئین های بیرونی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Electrostatic interaction of positive charges on the surface of Psb31 with photosystem II in the diatom Chaetoceros gracilis Electrostatic interaction of positive charges on the surface of Psb31 with photosystem II in the diatom Chaetoceros gracilis](/preview/png/5507134.png)
چکیده انگلیسی
Psb31, a novel extrinsic protein found in diatom photosystem II (PSII), directly binds to PSII core subunits, independent of the other extrinsic proteins, and functions to maintain optimum oxygen evolution. However, how Psb31 electrostatically interacts with PSII intrinsic proteins remains to be clarified. In this study, we examined electrostatic interaction of Psb31 with PSII complexes isolated from the diatom Chaetoceros gracilis. Positive or negative charges of isolated Psb31 proteins were modified with N-succinimidyl propionate (NSP) or glycine methyl ester (GME), respectively, resulting in formation of uncharged groups. NSP-modified Psb31 did not bind to PSII with a concomitant increase in NSP concentration, whereas GME-modified Psb31 clearly bound to PSII with retention of oxygen-evolving activity, indicating that positive charges of Lys residues and the N-terminus on the surface of Psb31 are involved in electrostatic interactions with PSII intrinsic proteins. Mass spectrometry analysis of NSP-modified Psb31 and sequence comparisons of Psb31 from C. gracilis with other chromophyte algae led to identification of three Lys residues as possible binding sites to PSII. Based on these findings, together with our previous cross-linking study in diatom PSII and a red algal PSII structure, we discuss binding properties of Psb31 with PSII core proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1858, Issue 9, September 2017, Pages 779-785
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1858, Issue 9, September 2017, Pages 779-785
نویسندگان
Ryo Nagao, Takehiro Suzuki, Akinori Okumura, Tomohiro Kihira, Ayaka Toda, Naoshi Dohmae, Katsuyoshi Nakazato, Tatsuya Tomo,