Homologous recombination in the Dictyostelium alpha-actinin gene leads to an altered mRNA and lack of the protein.
Open Access
- 20 December 1987
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 6 (13) , 4143-4148
- https://doi.org/10.1002/j.1460-2075.1987.tb02760.x
Abstract
Mutation of the alpha‐actinin gene in Dictyostelium has been achieved by transforming cells with the Dictyostelium transformation vector pDNeoII containing a 1.2 kb fragment of the alpha‐actinin gene. Transformants deficient in alpha‐actinin, an actin‐binding protein, produced an altered mRNA that lacked the 3′ portion of the coding region. The defect in alpha‐actinin production was not due to integration of the vector within the gene, but was apparently caused by errors produced during homologous recombination between the introduced alpha‐actinin sequence and its complementary sequence in the coding region of the endogenous gene.This publication has 24 references indexed in Scilit:
- Calcium‐sensitive non‐muscle α‐actinin contains EF‐hand structures and highly conserved regionsFEBS Letters, 1987
- Disruption of the Dictyostelium Myosin Heavy Chain Gene by Homologous RecombinationScience, 1987
- Introduction of homologous DNA sequences into mammalian cells induces mutations in the cognate geneNature, 1986
- Studies on the transcription, translation, and structure of alpha-actinin in Dictyostelium discoideum.The Journal of cell biology, 1986
- High frequency targeting of genes to specific sites in the mammalian genomeCell, 1986
- Phenocopy of discoidin I-minus mutants by antisense transformation in DictyosteliumCell, 1985
- Organization of the Dictyostelium discoideum actin multigene familyJournal of Molecular Biology, 1985
- The ubiquitin‐mediated proteolytic pathway and mechanisms of energy‐dependent intracellular protein degradationJournal of Cellular Biochemistry, 1984
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970