A high degree of homology exists between the protein encoded by SLG and the S receptor domain encoded by SRK in self-incompatible Brassica campestris L.
A high degree of homology exists between the protein encoded by SLG and the S receptor domain encoded by SRK in self-incompatible Brassica campestris L.
复制标题
自交不亲和油菜SLG编码的蛋白与SRK编码的S受体结构域之间存在高度的同源性。
DOI：
10.1093/oxfordjournals.pcp.a078716
复制
发表时间：
1994
影响因子：
4.9
通讯作者：
K. Hinata
中科院分区：
文献类型：
--
作者：
M. Watanabe;T. Takasaki;K. Toriyama;S. Yamakawa;A. Isogai;A. Suzuki;K. Hinata
白菜型油菜孢子体自交不亲和性系统是由一个基因座S的多等位基因控制的。我们从S9纯合子菌株中分离并鉴定了对应于S-糖蛋白（SLG）和S-受体激酶（SRK）基因的cDNA克隆。通过聚合酶链反应（PCR），使用对应于细胞外受体结构域（S-结构域）和激酶结构域的基因区域的引物扩增SRK 9片段。以该片段为探针，从一株S9纯合子柱头cDNA文库中分离得到SRK 9 cDNA克隆。以SLG 8 cDNA为探针，从文库中分离到SLG 9 cDNA克隆。限制性片段长度多态性（RFLP）连锁分析的F2植物从S8 S9杂交表明，SRK和SLG基因紧密连锁彼此，也与S-基因型，授粉试验确定。SRK 9和SLG 9的转录本在柱头中检测到，而在花药和叶片中未检测到。SRK 9编码的胞质激酶结构域含有丝氨酸/苏氨酸激酶中保守的氨基酸序列。SRK 9的S结构域与SLG 9的S结构域的核苷酸同源性为98.4%。这一观察结果表明，存在一种机制，用于保持SLG和SRK的S-结构域编码区域之间的高度相似性。
The sporophytic self-incompatibility system in Brassica campestris is controlled by multiple alleles of a single locus, S. We isolated and characterized cDNA clones that correspond to genes for S-glycoprotein (SLG) and S-receptor kinase (SRK) from an S9-homozygous strain. An SRK9 fragment was amplified by the polymerase chain reaction (PCR) by use of primers that corresponded to regions of the gene for the extracellular receptor domain (S-domain) and the kinase domain. The fragment was used as a probe to isolate an SRK9 cDNA clone from the cDNA library of stigmas of an S9-homozygote. An SLG9 cDNA clone was also isolated from the library by use of SLG8 cDNA as a probe. Restriction fragment length polymorphism (RFLP) linkage analysis of the F2 plants from an S8S9 hybrid demonstrated that the SRK and SLG genes were tightly linked to one another and were also linked to S-genotypes, as determined by pollination tests. The transcripts of SRK9 and SLG9 were detected in stigmas, but not in anthers or leaves. The cytoplasmic kinase domain encoded by SRK9 contained amino acid sequences that are conserved in serine/threonine kinases. The nucleotide sequence encoding the S-domain of SRK9 was 98.4% homologous to that of SLG9 at the nucleotide level. This observation suggests the existence of a mechanism for maintaining a high degree of similarity between SLG and the region that encodes the S-domain of SRK.