Grauso M, Culetto E, Berge J B, Toutant J P, Arpagaus M
Différenciation Cellulaire et Croissance, INRA, Montpellier, France.
DNA Seq. 1996;6(4):217-27. doi: 10.3109/10425179609008446.
The ace-1 gene, which encodes acetylcholinesterase of class A, has been cloned and sequenced in C. briggsae and compared to its homologue in C. elegans. Both genes present an open reading frame of 1860 nucleotides. The percentages of identity are 80% and 95% at the nucleotide and aminoacid levels respectively. All residues characteristic of an acetylcholinesterase are found in conserved positions in C. briggsae ACE-1. The deduced C-terminus is hydrophilic, thus resembling the catalytic peptide T of vertebrate cholinesterases. Codon usage in both ace-1 genes appears to be lowly biased. This may indicate that these genes are lowly expressed. The splicing sites of the eight introns of ace-1 in C. elegans are conserved in C. briggsae, but introns are shorter in C. briggsae. No homology was found between intronic sequences in both species, except for the consensus border sequences.
编码A类乙酰胆碱酯酶的ace-1基因已在秀丽隐杆线虫中克隆并测序，并与其在秀丽隐杆线虫中的同源物进行了比较。两个基因都有一个1860个核苷酸的开放阅读框。核苷酸和氨基酸水平的同一性百分比分别为80%和95%。乙酰胆碱酯酶的所有特征性残基都位于秀丽隐杆线虫ACE-1的保守位置。推导的C末端是亲水的，因此类似于脊椎动物胆碱酯酶的催化肽T。两个ace-1基因的密码子使用似乎偏向性较低。这可能表明这些基因表达水平较低。秀丽隐杆线虫中ace-1的八个内含子的剪接位点在秀丽隐杆线虫中是保守的，但秀丽隐杆线虫中的内含子较短。除了共有边界序列外，两个物种的内含子序列之间未发现同源性。
