Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences.

Understanding Plant Cellulose Synthases through a Comprehensive Investigation of the Cellulose Synthase Family Sequences.
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通过全面研究纤维素合酶家族序列,了解植物纤维素合成酶。

DOI:
10.3389/fpls.2011.00005
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发表时间:
2011
影响因子:
5.6
通讯作者:
Specht CD
Specht CD
中科院分区:
生物学2区
文献类型:
--
作者:
Carroll A;Specht CD

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纤维素作为植物细胞壁中的组织结构的发展是维管植物最初定殖和随后统治陆地生态系统的关键事件。大量的实验数据已经证明了形成合成纤维素的大型合成复合物所需的复杂的遗传相互作用。然而,这些结果缺乏对组成这种复合物的蛋白质的进化,专业化和调控的广泛分析。在这里,我们进行了深入的分析纤维素合酶(CesA)家族的序列。我们调查的CesA家族的遗传,强调进化专业化。我们定义专门的分支,并确定类特定的区域内的CesA序列,可以解释这种专业化。我们调查的变化,在监管中的CesAs的保护建议的磷酸化位点。我们研究了已记录的突变损害CesA功能的位点的保守性,并将这些位点与最接近的纤维素酶样(Csl)家族中观察到的位点进行比较,以更好地了解哪些区域可以将CesA与其他Csl分开。最后,我们确定了两个位置具有很强的保守性的芳香性状,但缺乏保守的氨基酸身份,这可能代表残基的重要定位的糖底物催化。这些分析提供了有用的工具,了解特征的突变和翻译后修饰,并通知进一步的实验,以探测CesA的组装,调节和功能,通过定点诱变或结构域交换实验。
The development of cellulose as an organizing structure in the plant cell wall was a key event in both the initial colonization and the subsequent domination of the terrestrial ecosystem by vascular plants. A wealth of experimental data has demonstrated the complicated genetic interactions required to form the large synthetic complex that synthesizes cellulose. However, these results are lacking an extensive analysis of the evolution, specialization, and regulation of the proteins that compose this complex. Here we perform an in-depth analysis of the sequences in the cellulose synthase (CesA) family. We investigate the phylogeny of the CesA family, with emphasis on evolutionary specialization. We define specialized clades and identify the class-specific regions within the CesA sequence that may explain this specialization. We investigate changes in regulation of CesAs by looking at the conservation of proposed phosphorylation sites. We investigate the conservation of sites where mutations have been documented that impair CesA function, and compare these sites to those observed in the closest cellulose synthase-like (Csl) families to better understand what regions may separate the CesAs from other Csls. Finally we identify two positions with strong conservation of the aromatic trait, but lacking conservation of amino acid identity, which may represent residues important for positioning the sugar substrate for catalysis. These analyses provide useful tools for understanding characterized mutations and post-translational modifications, and for informing further experiments to probe CesA assembly, regulation, and function through site-directed mutagenesis or domain swapping experiments.
DOI: 10.1073/pnas.89.22.10915
发表时间: 1992-11-15
影响因子: 11.1
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