Expression of GFP-mTalin reveals an actin-related role for the Arabidopsis Class II formin AtFH12.
Cvrčková F., Grunt M., Žárský V.
BIOLOGIA PLANTARUM 56: 431-440, 2012
Keywords: FH2 proteins, genetic redundancy, salt stress, synthetic lethality
Abstract: Formins (FH2 proteins) are implicated in F-actin nucleation and other aspects of cytoskeletal organization. Plants possess two formin clades, relatively well-described Class I formins and so far poorly characterized Class II formins. Comparison of Class II formin genes of two Arabidopsis species, A. thaliana and A. lyrata, indicates dynamic evolution within the Class II formin clade. Disruption of an outlier A. thaliana Class II formin gene, AtFH12 (At1g42980), whose expression is induced by NaCl, produced only negligible phenotypic effects under a variety of conditions, including salt stress, suggesting functional redundancy among Class II formins. However, the same mutation massively aggravated toxic effects of the expression of a fluorescent actin marker, GFP-tagged mouse talin (GFP-mTalin), known to interfere with normal actin dynamics. Abnormal actin structures were observed in atfh12 mutants expressing GFP-mTalin as compared to wild type. This not only demonstrates an actin-associated function for AtFH12, but also documents the feasibility of using the heterologous actin marker to “stress-test” the actin cytoskeleton in phenotyping “weak“ actin related mutant alleles.
DOI: IEB authors: Viktor Žárský
BIOLOGIA PLANTARUM 56: 431-440, 2012
Keywords: FH2 proteins, genetic redundancy, salt stress, synthetic lethality
Abstract: Formins (FH2 proteins) are implicated in F-actin nucleation and other aspects of cytoskeletal organization. Plants possess two formin clades, relatively well-described Class I formins and so far poorly characterized Class II formins. Comparison of Class II formin genes of two Arabidopsis species, A. thaliana and A. lyrata, indicates dynamic evolution within the Class II formin clade. Disruption of an outlier A. thaliana Class II formin gene, AtFH12 (At1g42980), whose expression is induced by NaCl, produced only negligible phenotypic effects under a variety of conditions, including salt stress, suggesting functional redundancy among Class II formins. However, the same mutation massively aggravated toxic effects of the expression of a fluorescent actin marker, GFP-tagged mouse talin (GFP-mTalin), known to interfere with normal actin dynamics. Abnormal actin structures were observed in atfh12 mutants expressing GFP-mTalin as compared to wild type. This not only demonstrates an actin-associated function for AtFH12, but also documents the feasibility of using the heterologous actin marker to “stress-test” the actin cytoskeleton in phenotyping “weak“ actin related mutant alleles.
DOI: IEB authors: Viktor Žárský