Single Amino Acid Exchanges in Separate Domains of the Drosophila serendipity {delta} Zinc Finger Protein Cause Embryonic and Sex Biased Lethality

Single Amino Acid Exchanges in Separate Domains of the Drosophila serendipity {delta} Zinc Finger... M. Crozatier, K. Kongsuwan, P. Ferrer, J. R. Merriam, J. A. Lengyel and A. Vincent Centre de Recherche de Biochimie et de Genetique Cellulaires du CNRS 118, route de Narbonne, 31062 Toulouse Cedex, France The Drosophila serendipity (sry) delta ({delta}) zinc finger protein is a sequence-specific DNA binding protein, maternally inherited by the embryo and present in nuclei of transcriptionally active cells throughout fly development. We report here the isolation and characterization of four ethyl methanesulfate-induced zygotic lethal mutations of different strengths in the sry {delta} gene. For the stronger allele, all of the lethality occurs during late embryogenesis or the first larval instar. In the cases of the three weaker alleles, most of the lethality occurs during pupation; moreover, those adult escapers that emerge are sterile males lacking partially or completely in spermatozoa bundles. Genetic analysis of sry {delta} thus indicates that it is an essential gene, whose continued expression throughout the life cycle, notably during embryogenesis and pupal stage, is required for viability. Phenotypic analysis of sry {delta} hemizygote escaper males further suggests that sry {delta} may be involved in regulation of two different sets of genes: genes required for viability and genes involved in gonadal development. All four sry {delta} alleles are fully rescued by a wild-type copy of sry {delta}, but not by an additional copy of the sry {beta} gene, reinforcing the view that, although structurally related, these two genes exert distinct functions. Molecular characterization of the four sry {delta} mutations revealed that these mutations correspond to single amino acid replacements in the sry {delta} protein. Three of these replacements map to the same (third out of seven) zinc finger in the carboxy-terminal DNA binding domain; interestingly, none affects the zinc finger consensus residues. The fourth mutation is located in the NH(2)-proximal part of the protein, in a domain proposed to be involved in specific protein-protein interactions. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Genetics Genetics Society of America

Single Amino Acid Exchanges in Separate Domains of the Drosophila serendipity {delta} Zinc Finger Protein Cause Embryonic and Sex Biased Lethality

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Publisher
Genetics Society of America
Copyright
Copyright © 1992 by the Genetics Society of America
ISSN
0016-6731
eISSN
1943-2631
Publisher site
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Abstract

M. Crozatier, K. Kongsuwan, P. Ferrer, J. R. Merriam, J. A. Lengyel and A. Vincent Centre de Recherche de Biochimie et de Genetique Cellulaires du CNRS 118, route de Narbonne, 31062 Toulouse Cedex, France The Drosophila serendipity (sry) delta ({delta}) zinc finger protein is a sequence-specific DNA binding protein, maternally inherited by the embryo and present in nuclei of transcriptionally active cells throughout fly development. We report here the isolation and characterization of four ethyl methanesulfate-induced zygotic lethal mutations of different strengths in the sry {delta} gene. For the stronger allele, all of the lethality occurs during late embryogenesis or the first larval instar. In the cases of the three weaker alleles, most of the lethality occurs during pupation; moreover, those adult escapers that emerge are sterile males lacking partially or completely in spermatozoa bundles. Genetic analysis of sry {delta} thus indicates that it is an essential gene, whose continued expression throughout the life cycle, notably during embryogenesis and pupal stage, is required for viability. Phenotypic analysis of sry {delta} hemizygote escaper males further suggests that sry {delta} may be involved in regulation of two different sets of genes: genes required for viability and genes involved in gonadal development. All four sry {delta} alleles are fully rescued by a wild-type copy of sry {delta}, but not by an additional copy of the sry {beta} gene, reinforcing the view that, although structurally related, these two genes exert distinct functions. Molecular characterization of the four sry {delta} mutations revealed that these mutations correspond to single amino acid replacements in the sry {delta} protein. Three of these replacements map to the same (third out of seven) zinc finger in the carboxy-terminal DNA binding domain; interestingly, none affects the zinc finger consensus residues. The fourth mutation is located in the NH(2)-proximal part of the protein, in a domain proposed to be involved in specific protein-protein interactions.

Journal

GeneticsGenetics Society of America

Published: Aug 1, 1992

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