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首页> 外文期刊>RSC Advances >Occurrence of a functionally stable photoharvesting single peptide allophycocyanin alpha-subunit (16.4 kDa) in the cyanobacterium Nostoc sp R76DM
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Occurrence of a functionally stable photoharvesting single peptide allophycocyanin alpha-subunit (16.4 kDa) in the cyanobacterium Nostoc sp R76DM

机译：在骨杆菌SP r76dm中，在Cyanobacterium sp r76dm中发生功能稳定的聚蛋白单肽聚苯单蛋白α-亚基（16.4kDa）

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摘要

Allophycocyanin (APC) is a primary photoreceptor, usually composed of alpha- and beta-polypeptide subunits. Herein, we report the occurrence of a functionally stable single peptide APC alpha-subunit in cyanobacterium Nostoc sp. R76DM. APC was purified successfully by ammonium sulfate fractionation. A series of biochemical characterizations like SDS-PAGE, native-PAGE, UV-visible spectroscopy, fluorescence spectroscopy and circular dichroism were performed to ensure the purity, integrity and functionality of the purified APC. Matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis of intact PBP revealed a similar to 16.4 kDa protein. The MS/MS spectrum of five major peptides 1051, 1431, 936, 2291 and 2163 Da of trypsin digested purified PBP, followed by amino acid sequences of these peptides, shows a high degree (100%) of sequence similarities with that of the APC alpha-subunit (accession no. P16570, UniProtKB). The absorption as well as the fluorescence spectra of a single peptide APC alpha-subunit was shifted from normal absorption at 652 nm to 613 nm, and fluorescence at 663 nm to 645 nm. Urea-induced denaturation based Gibbs-free energy (Delta G(D)degrees) calculations suggested that the folding and structural stability of the APC alpha-subunit is almost similar to that of the standard APC (alpha beta) heterodimer from Lyngbya sp. Moreover, due to its conserved structural and functional integrity, the APC alpha-subunit may be widely used as a relatively low molecular weight fluorescent tag for fluorescence detection techniques.
机译：联素胶质素（APC）是初级光感受器，通常由α-和β-多肽亚基组成。在此，我们报告在骨杆菌杆菌SP中的功能稳定的单肽APCα-亚基的发生。 R76DM。通过硫酸铵分级成功纯化APC。进行一系列生化特征，如SDS-PAGE，本机 - 页面，UV可见光谱，荧光光谱和圆形二色性，以确保纯化APC的纯度，完整性和官能度。基质辅助激光解吸电离飞行时间质谱（MALDI-TOF-MS）完整PBP的分析显示出类似于16.4kDa蛋白。胰蛋白酶消化纯化的PBP的五个主要肽1051,1431,936,2291和2163Da的MS / MS光谱，其次是这些肽的氨基酸序列，显示出具有APC的高度（100％）的序列相似性alpha-sub单元（登录号P16570，UniProtkb）。单肽APCα-亚基的吸收以及荧光光谱从652nm至613nm的正常吸收移位，荧光为663nm至645nm。尿素诱导的基于去饱和的Gibbs - 无糖型能量（Delta G（d）度）计算表明APCα-亚基的折叠和结构稳定性几乎类似于来自Lyngbya Sp的标准APC（αβ）异二聚体的折叠和结构稳定性。此外，由于其保守的结构和功能完整性，APCα-亚基可以广泛用作荧光检测技术的相对低的分子量荧光标签。

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  • 来源
    《RSC Advances》 |2015年第106期|共11页
  • 作者

    Rastogi Rajesh P.; Sonani Ravi R.; Patel Avani B.; Madamwar Datta;

  • 作者单位

    Sardar Patel Univ BRD Sch Biosci Vallabh Vidyanagar 388120 Gujarat India;

    Sardar Patel Univ BRD Sch Biosci Vallabh Vidyanagar 388120 Gujarat India;

    Sardar Patel Univ BRD Sch Biosci Vallabh Vidyanagar 388120 Gujarat India;

    Sardar Patel Univ BRD Sch Biosci Vallabh Vidyanagar 388120 Gujarat India;

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  • 正文语种 eng
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