Human Protein NEFA, a Novel DNA Binding / EF-Hand / Leucine Zipper Protein. Molecular Cloning and Sequence Analysis of the cDNA, Isolation and Characterization of the Protein.

1994 ◽  
Vol 375 (8) ◽  
pp. 497-512 ◽  
Author(s):  
Shitsu Barnikol-Watanabe ◽  
Nikola A. Groß ◽  
Hilde Götz ◽  
Thomas Henkel ◽  
Anton Karabinos ◽  
...  
2020 ◽  
Vol 27 (6) ◽  
pp. 1562-1565
Author(s):  
Eijaz Ahmed Bhat ◽  
Nasreena Sajjad ◽  
Jamal S.M. Sabir ◽  
Majid Rasool Kamli ◽  
Khalid Rehman Hakeem ◽  
...  

2013 ◽  
Vol 1 (3) ◽  
pp. 236-244 ◽  
Author(s):  
Hyoshin Lee ◽  
Eung-Jun Park ◽  
Seo-Kyung Yoon ◽  
Mi Na Choi ◽  
Soo Hyung Eo

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.


1986 ◽  
Vol 367 (2) ◽  
pp. 803-812 ◽  
Author(s):  
Johannes DODT ◽  
Werner MACHLEIDT ◽  
Ursula SEEMÜLLER ◽  
Reinhard MASCHLER ◽  
Hans FRITZ

1993 ◽  
Vol 293 (1) ◽  
pp. 21-25 ◽  
Author(s):  
A C F Perry ◽  
R Jones ◽  
L Hall

Superoxide dismutase (SOD) plays a key role in combating loss of fertility of spermatozoa due to lipid peroxidation. Here we report the sequence of a cDNA encoding a secreted form of SOD isolated from a rat epididymal library. Northern-blot analysis indicates that the corresponding transcript is expressed principally in the cauda region of the epididymis, consistent with the high levels of SOD enzyme activity found in cauda-epididymidal plasma. Much lower levels of an identically sized transcript exist in all tissues examined, including placenta. PCR and subsequent sequence analysis of rat placental SOD strongly suggest that it is identical in sequence with epididymal SOD.


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