Arabinogalactan-Proteins as Boron-Acting Enzymes, Cross-Linking the Rhamnogalacturonan-II Domains of Pectin.

Arabinogalactan-Proteins as Boron-Acting Enzymes, Cross-Linking the Rhamnogalacturonan-II Domains of Pectin.
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作为硼作用酶的阿拉伯半乳聚糖-蛋白质,交联果胶的鼠李半乳糖醛酸-II结构域。

DOI:
10.3390/plants12233921
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发表时间:
2023-11-21
期刊:
Plants (Basel, Switzerland)
影响因子:
--
通讯作者:
Fry SC
Fry SC
中科院分区:
其他
文献类型:
--
作者:
Begum RA;Fry SC

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植物细胞壁中的大多数果胶鼠李糖半乳糖醛酸-II(RG-II)结构域是硼酸盐桥接的二聚体。然而,亚细胞位置,pH依赖性,可逆性和生物催化剂参与硼酸盐桥接仍然不确定。这里讨论的实验探讨了这些问题,利用悬浮培养的植物细胞。体内脉冲放射性标记显示,大多数RG-II结构域非常快速地二聚化(生物合成后<4分钟,因此仍在原生质内)。这与硼提取导致细胞壁在10-20分钟内弱化的发现相吻合,并支持先前提出的硼/RG-II复合物在壁/膜界面处的生物作用。我们还讨论了RG-II单体Particip-dimer相互转化监测在体外使用凝胶电泳和一种新的薄层色谱法来解决单体和二聚体。生理相关的酸度没有monomerise二聚体,因此硼桥断裂不能在“酸生长”的壁松动机制,然而,最近发现的RG-II三聚体和四聚体是不稳定的,因此可能支持可逆的壁松动。通过B(OH)3在体外使单体二聚需要同时存在RG-II结合“伴侣”:配位结合金属和/或离子结合阳离子肽。后一种类型的天然分子伴侣包括高度碱性的阿拉伯半乳聚糖蛋白片段,例如,KHKRKHKHKRHHH,其催化反应[2 RG-II + B(OH)3 → RG-II-B-RG-II],表明植物可以“酶促”代谢硼。
Most pectic rhamnogalacturonan-II (RG-II) domains in plant cell walls are borate-bridged dimers. However, the sub-cellular locations, pH dependence, reversibility and biocatalyst involvement in borate bridging remain uncertain. Experiments discussed here explored these questions, utilising suspension-cultured plant cells. In-vivo pulse radiolabelling showed that most RG-II domains dimerise extremely quickly (<4 min after biosynthesis, thus while still intraprotoplasmic). This tallies with the finding that boron withdrawal causes cell wall weakening within 10–20 min, and supports a previously proposed biological role for boron/RG-II complexes specifically at the wall/membrane interface. We also discuss RG-II monomer ↔ dimer interconversion as monitored in vitro using gel electrophoresis and a novel thin-layer chromatography method to resolve monomers and dimers. Physiologically relevant acidity did not monomerise dimers, thus boron bridge breaking cannot be a wall-loosening mechanism in ‘acid growth’; nevertheless, recently discovered RG-II trimers and tetramers are unstable and may thus underpin reversible wall loosening. Dimerising monomers in vitro by B(OH)3 required the simultaneous presence of RG-II-binding ‘chaperones’: co-ordinately binding metals and/or ionically binding cationic peptides. Natural chaperones of the latter type include highly basic arabinogalactan protein fragments, e.g., KHKRKHKHKRHHH, which catalyse a reaction [2 RG-II + B(OH)3 → RG-II–B–RG-II], suggesting that plants can ‘enzymically’ metabolise boron.
DOI: 10.1111/nph.14897
发表时间: 2018-03
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影响因子: --
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