Characterization of a null mutation in ace-1, the gene encoding class A acetylcholinesterase in the nematode Caenorhabditis elegans

• Published in: FEBS letters Vol. 357; no. 3; pp. 265 - 268
• Main Authors: Talesa, Vincenzo, Culetto, Emmanuel, Schirru, Nathalie, Bernardi, Henri, Fedon, Yann, Toutant, Jean-Pierre, Arpagaus, Martine
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 09-01-1995; Wiley
• Subjects: Acetylcholinesterase; Acetylcholinesterase - genetics; Animals; Base Sequence; Caenorhabditis elegans; Caenorhabditis elegans - enzymology; Computer Science; Genes, Helminth; Life Sciences; Molecular Sequence Data; mRNA stability; Mutation; Nematode; Null mutation; Oligodeoxyribonucleotides; RNA, Messenger - genetics; RNA, Messenger - metabolism; Null mutation; Caenorhabditis elegans; Nematode; Acetylcholinesterase; mRNA stability
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)01343-Y

Two genes (
ace-1 and
ace-2) encode two major classes (A and B) of acetylcholinesterase (AChE) in the nematode
Caenorhabditis elegans. A null mutation in
ace-1 (allele
p1000) suppresses all acetylcholinesterase activity of class A. We have identified an opal mutation TG
G
(W99)→TG
A
(Stop) as the only alteration in the mutated gene. This leads to a truncated protein (98 instead of 620 amino acids) with no enzymatic activity. The mutation also reduces the level of
ace-1 transcripts to only 10% of that in wild-type animals. This most likely results from a destabilization of mRNA containing the nonsense message. In contrast, compensation of class B by class A AChE in the null mutant strain
ace-2 takes place with unchanged
ace-1 mRNA level and enzymatic activity similar to class A AChE.