1Instituto de Agrobiotecnología y Biología Molecular-IABiMo-INTA-CONICET, Instituto de Biotecnología, Centro de Investigaciones en Ciencias Veterinarias y Agronómicas, Instituto Nacional de Tecnología Agropecuaria, Hurlingham, Argentina
2Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Argentina
3Departamento de Fisiología, Biología Molecular y Celular (FBMC), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos, Ciudad Universitaria, Buenos Aires, Argentina
*Corresponding author:Flavia Soledad Darqui, Instituto de Agrobiotecnología y Biología Molecular-IABiMo-INTA-CONICET, Instituto de Biotecnología, Centro de Investigaciones en Ciencias Veterinarias y Agronómicas, Instituto Nacional de Tecnología Agropecuaria, Nicolás Repetto y De Los Reseros S/Nº (B1686IGC) Hurlingham, Buenos Aires, Argentina
Submission: July 15, 2020;Published: August 31, 2020
ISSN: 2637-7659 Volume7 Issue2
Specific mutations in the conserved domains of the acetolactate synthase (ALS) gene conduct to different key amino acid substitutions that can confer herbicide resistance in different plant species. This outcome has been widely exploited to produce herbicide-resistant agronomic crops as well as to direct many genome editing studies. Therefore, the ALS gene has become a model sequence target to improve our technological skills for more precise CRISPR/Cas nucleotide base substitution in plants, which is essential for modulation/modification of gene function as opposed to the more general gene knock out obtained by indels in conventional genome editing studies. This review summarizes the main knowledge and experiences attained from the use of the ALS gene as a target in CRISPR/Cas studies.
Keywords: Acetolactate synthase; Targeted mutagenesis; Gene targeting; Base editing
Abbreviations: ALS: Acetolactate Synthase; AAS: Amino Acid Substitutions; CBE: cytosine base Editor; DSBs: Double-Strand Breaks; GE: Genome Editing; HDR: Homology-Directed Repair; NHEJ: Non-Homologous End-Joining; RT: Repair Template; SSN: Sequence-Specific Nuclease