scholarly journals Identification and characterization of a salt stress-inducible zinc finger protein from Festuca arundinacea

2012 ◽  
Vol 5 (1) ◽  
Author(s):  
Ruth C Martin ◽  
Kira Glover-Cutter ◽  
James C Baldwin ◽  
James E Dombrowski
2012 ◽  
Vol 39 (6) ◽  
pp. 6513-6519 ◽  
Author(s):  
Sávio Pinho dos Reis ◽  
Liliane de Souza Conceição Tavares ◽  
Carinne de Nazaré Monteiro Costa ◽  
Aílton Borges Santa Brígida ◽  
Cláudia Regina Batista de Souza

Genomics ◽  
2000 ◽  
Vol 65 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Kazuhiro Yano ◽  
Nobuhide Ueki ◽  
Tamaki Oda ◽  
Naohiko Seki ◽  
Yasuhiko Masuho ◽  
...  

2018 ◽  
Vol 501 (4) ◽  
pp. 920-926 ◽  
Author(s):  
Ruixiang Zhang ◽  
Jian Li ◽  
Manyu Xiang ◽  
Qinghua Hong ◽  
Bin Xu ◽  
...  

Genetics ◽  
1992 ◽  
Vol 131 (4) ◽  
pp. 905-916 ◽  
Author(s):  
M Crozatier ◽  
K Kongsuwan ◽  
P Ferrer ◽  
J R Merriam ◽  
J A Lengyel ◽  
...  

Abstract 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 NH2-proximal part of the protein, in a domain proposed to be involved in specific protein-protein interactions.


1995 ◽  
Vol 28 (2) ◽  
pp. 267-279 ◽  
Author(s):  
Brian W. Tague ◽  
Howard M. Goodman

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