The tomato / gene for Fusarium wilt resistance encodes an atypical leucine-rich repeat receptor-like protein whose function is nevertheless dependent on SOBIR1 and SERK3/BAK1
The tomato / gene for Fusarium wilt resistance encodes an atypical leucine-rich repeat receptor-like protein whose function is nevertheless dependent on SOBIR1 and SERK3/BAK1
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DOI：
10.1111/tpj.13458
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发表时间：
2017-03-01
期刊：
影响因子：
7.2
通讯作者：
Jones, David A.
中科院分区：
文献类型：
--
作者：
Catanzariti, Ann-Maree;Do, Huong T. T.;Jones, David A.
我们已经鉴定出番茄I基因对枯萎病真菌Fusarium oxysporum f. sp. lycopersici （Fol）的抗性，并表明它编码一个膜固定的富含亮氨酸的重复受体样蛋白（LRR-RLP）。与大多数其他参与植物防御的LRR-RLP基因不同，I基因不是基因簇的成员，其编码序列中含有内含子。I基因编码一个比大多数其他lrr - rlp更大的环域，具有丰富的丝氨酸和苏氨酸残基的独特组成。I蛋白也缺乏一个基本的细胞质结构域。相反，这个结构域富含芳香残基，可以形成第二个跨膜结构域。I蛋白识别Fol Avr1效应蛋白，但与许多其他lrrrlp不同的是，识别特异性是在蛋白质的c端一半由环出结构域之前的LRRs和环出结构域本身的多态性氨基酸残基决定的。尽管存在这些差异，但我们发现，本烟的I/ avr1依赖性坏死依赖于LRR受体样激酶（rlk） SERK3/BAK1和SOBIR1。序列比较表明，I蛋白和其他参与植物防御的LRR- rlp在其最后LRR和c端LRR capping域中均携带与SERK3/ bak1相互作用残基在LRR- rlks BRI1和PSKR1中相同相对位置的保守残基。其中两个保守残基Q922和T925的酪氨酸突变，消除了benthamiana中I/ avr1依赖性坏死，与BRI1和PSKR1的类似突变一致，阻止了它们与SERK3/BAK1的相互作用。
We have identified the tomato I gene for resistance to the Fusarium wilt fungus Fusarium oxysporum f. sp. lycopersici (Fol) and show that it encodes a membrane-anchored leucine-rich repeat receptor-like protein (LRR-RLP). Unlike most other LRR-RLP genes involved in plant defence, the I gene is not a member of a gene cluster and contains introns in its coding sequence. The I gene encodes a loopout domain larger than those in most other LRR-RLPs, with a distinct composition rich in serine and threonine residues. The I protein also lacks a basic cytosolic domain. Instead, this domain is rich in aromatic residues that could form a second transmembrane domain. The I protein recognises the Fol Avr1 effector protein, but, unlike many other LRRRLPs, recognition specificity is determined in the C-terminal half of the protein by polymorphic amino acid residues in the LRRs just preceding the loopout domain and in the loopout domain itself. Despite these differences, we show that I/Avr1-dependent necrosis in Nicotiana benthamiana depends on the LRR receptor-like kinases (RLKs) SERK3/BAK1 and SOBIR1. Sequence comparisons revealed that the I protein and other LRR-RLPs involved in plant defence all carry residues in their last LRR and C-terminal LRR capping domain that are conserved with SERK3/BAK1-interacting residues in the same relative positions in the LRR-RLKs BRI1 and PSKR1. Tyrosine mutations of two of these conserved residues, Q922 and T925, abolished I/Avr1-dependent necrosis in N. benthamiana, consistent with similar mutations in BRI1 and PSKR1 preventing their interaction with SERK3/BAK1.