Wright C S, Raikhel N
Department of Biochemistry and Molecular Biophysics, Medical College of Virginia/Virginia Commonwealth University, Richmond 23298-0001.
J Mol Evol. 1989 Apr;28(4):327-36. doi: 10.1007/BF02103429.
Three highly homologous wheat germ isolectins (95-97%) are distinct gene products in hexaploid wheat. The amino acid sequences of two of these [wheat germ agglutinin 1 (WGA1) and 2 (WGA2)] are compared with sequence data derived from a complementary DNA (cDNA) clone for the third isolectin (WGA3). This comparison includes three corrections to earlier amino acid sequence data of both WGA1 and WGA2 at positions 109 (from Ser to Phe), 134 (from Gly to Lys), and 150 (from Gly to Trp). These reassignments are based on new results from crystal structure refinement and amino acid sequence data of WGA1, as well as the recently determined nucleotide sequence of WGA3. In addition, the C-terminal residue of WGA1 has been revised to Gly171 and now differs from WGA2 (Ala171). Four other positions, Asn9, Ala53, Gly119, and Ser123, at which WGA1 and WGA2 are identical but differ from the DNA sequence of WGA3, were also reinvestigated by amino acid sequencing techniques and confirmed. Variability among the three isolectins is observed at a total of 10 sequence positions: 9, 53, 56, 59, 66, 93, 109, 119, 123, and 171. Pairwise comparisons indicate that WGA3 deviates to a much larger extent from WGA1 (at eight positions) and from WGA2 (at seven positions) than the latter from one another (at five positions). Eight of the 10 mutations are equally distributed between domains B and C, the two interior and more highly conserved of the four WGA domains (A, B, C, D). Correlation of the variable residues with the three-dimensional structure indicates that all except the two previously described B-domain residues, 56 and 59 (Wright and Olafsdottir 1986), are easily accommodated at the dimer surface. WGA3 displays a higher degree of inter-domain similarity than found in WGA1 and WGA2. Of the seven variable positions that are located in the domain core (residues 3-31), five are in perfect agreement with our earlier predicted domain ancestor sequence. This suggests that of the three isolectins WGA3 is most closely related to the common ancestral molecule.
三种高度同源的小麦胚凝集素(同源性为95 - 97%)是六倍体小麦中不同的基因产物。将其中两种凝集素[小麦胚凝集素1(WGA1)和2(WGA2)]的氨基酸序列与从第三个凝集素(WGA3)的互补DNA(cDNA)克隆获得的序列数据进行比较。这种比较包括对WGA1和WGA2早期氨基酸序列数据在第109位(从丝氨酸变为苯丙氨酸)、134位(从甘氨酸变为赖氨酸)和150位(从甘氨酸变为色氨酸)的三处修正。这些重新赋值基于WGA1晶体结构优化的新结果和氨基酸序列数据,以及最近测定的WGA3核苷酸序列。此外,WGA1的C末端残基已修正为Gly171,现在与WGA2(Ala171)不同。另外四个位置,即Asn9、Ala53、Gly119和Ser123,WGA1和WGA2在此处相同,但与WGA3的DNA序列不同,也通过氨基酸测序技术进行了重新研究并得到证实。在总共10个序列位置观察到三种凝集素之间存在差异:9、53、56、59、66、93、109、119、123和171。成对比较表明,WGA3与WGA1(在八个位置)和WGA2(在七个位置)的偏差程度比WGA1和WGA2彼此之间的偏差程度(在五个位置)大得多。10个突变中的8个在结构域B和C之间平均分布,结构域B和C是四个WGA结构域(A、B、C、D)中两个内部且保守性更高的结构域。可变残基与三维结构的相关性表明,除了先前描述的两个B结构域残基56和59(Wright和Olafsdottir,1986)外,所有其他残基都很容易容纳在二聚体表面。WGA3显示出比WGA1和WGA2更高程度的结构域间相似性。在位于结构域核心(残基3 - 31)的七个可变位置中,有五个与我们早期预测的结构域祖先序列完全一致。这表明在三种凝集素中,WGA3与共同的祖先分子关系最为密切。