scholarly journals A novel missense variant in the GLI3 zinc finger domain in a family with digital anomalies

2017 ◽  
Vol 173 (12) ◽  
pp. 3221-3225 ◽  
Author(s):  
J. Aaron Crapster ◽  
Louanne Hudgins ◽  
James K. Chen ◽  
Natalia Gomez-Ospina
Keyword(s):  
Zinc Finger ◽  
Missense Variant ◽  
Zinc Finger Domain

Hsp70 Escort Protein: More Than a Regulator of Mitochondrial Hsp70

2018 ◽  
Vol 16 (1) ◽  
pp. 64-73 ◽  
Author(s):  
David O. Nyakundi ◽  
Stephen J. Bentley ◽  
Aileen Boshoff
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domain ◽  
C Terminus ◽  
Cellular Localisation ◽  
The Matrix ◽  
Mitochondrial Hsp70 ◽  
Cellular Compartments ◽  
Intramolecular Communication ◽  
Self Aggregation ◽  
J Protein

Hsp70 members occupy a central role in proteostasis and are found in different eukaryotic cellular compartments. The mitochondrial Hsp70/J-protein machinery performs multiple functions vital for the proper functioning of the mitochondria, including forming part of the import motor that transports proteins from the cytosol into the matrix and inner membrane, and subsequently folds these proteins in the mitochondria. However, unlike other Hsp70s, mitochondrial Hsp70 (mtHsp70) has the propensity to self-aggregate, accumulating as insoluble aggregates. The self-aggregation of mtHsp70 is caused by both interdomain and intramolecular communication within the ATPase and linker domains. Since mtHsp70 is unable to fold itself into an active conformation, it requires an Hsp70 escort protein (Hep) to both inhibit self-aggregation and promote the correct folding. Hep1 orthologues are present in the mitochondria of many eukaryotic cells but are absent in prokaryotes. Hep1 proteins are relatively small and contain a highly conserved zinc-finger domain with one tetracysteine motif that is essential for binding zinc ions and maintaining the function and solubility of the protein. The zinc-finger domain lies towards the C-terminus of Hep1 proteins, with very little conservation outside of this domain. Other than maintaining mtHsp70 in a functional state, Hep1 proteins play a variety of other roles in the cell and have been proposed to function as both chaperones and co-chaperones. The cellular localisation and some of the functions are often speculative and are not common to all Hep1 proteins analysed to date.

scholarly journals The ANGULATA 7 gene encodes a DnaJ‐like zinc finger‐domain protein involved in chloroplast function and leaf development in Arabidopsis

2017 ◽  
Vol 89 (5) ◽  
pp. 870-884 ◽  
Author(s):  
Tamara Muñoz‐Nortes ◽  
José Manuel Pérez‐Pérez ◽  
María Rosa Ponce ◽  
Héctor Candela ◽  
José Luis Micol
Keyword(s):  
Zinc Finger ◽  
Leaf Development ◽  
Zinc Finger Domain ◽  
Domain Protein

scholarly journals Crystal structure of zinc‐finger domain of Nanos and its functional implications

EMBO Reports ◽  
2010 ◽  
Vol 11 (11) ◽  
pp. 848-853 ◽  
Author(s):  
Hiroshi Hashimoto ◽  
Kodai Hara ◽  
Asami Hishiki ◽  
Shigeta Kawaguchi ◽  
Naoki Shichijo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Functional Implications

Characterization of the DNA Binding Activity of the ZFY Zinc Finger Domain

Biochemistry ◽  
2010 ◽  
Vol 49 (4) ◽  
pp. 679-686 ◽  
Author(s):  
Jennifer Grants ◽  
Erin Flanagan ◽  
Andrea Yee ◽  
Paul J. Romaniuk
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Activity ◽  
Zinc Finger Domain ◽  
Dna Binding Activity

scholarly journals The N-terminal zinc finger domain of Tgf2 transposase contributes to DNA binding and to transposition activity

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Xia-Yun Jiang ◽  
Fei Hou ◽  
Xiao-Dan Shen ◽  
Xue-Di Du ◽  
Hai-Li Xu ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Transposition Activity

Towards understanding the molecular recognition process in prokaryotic zinc-finger domain

2015 ◽  
Vol 91 ◽  
pp. 100-108 ◽  
Author(s):  
Luigi Russo ◽  
Maddalena Palmieri ◽  
Jolanda Valentina Caso ◽  
Gianluca D' Abrosca ◽  
Donatella Diana ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Recognition Process

scholarly journals Structural and Biochemical Characterization of Thioredoxin-2 from Deinococcus radiodurans

Antioxidants ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 1843
Author(s):  
Min-Kyu Kim ◽  
Lei Zhao ◽  
Soyoung Jeong ◽  
Jing Zhang ◽  
Jong-Hyun Jung ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Active Site ◽  
Biochemical Characterization ◽  
Deinococcus Radiodurans ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Antioxidant Systems ◽  
Zinc Finger Domain ◽  
Cxxc Motif ◽  
Reduction Activity ◽  
Trx Fold

Thioredoxin (Trx), a ubiquitous protein showing disulfide reductase activity, plays critical roles in cellular redox control and oxidative stress response. Trx is a member of the Trx system, comprising Trx, Trx reductase (TrxR), and a cognate reductant (generally reduced nicotinamide adenine dinucleotide phosphate, NADPH). Bacterial Trx1 contains only the Trx-fold domain, in which the active site CXXC motif that is critical for the disulfide reduction activity is located. Bacterial Trx2 contains an N-terminal extension, which forms a zinc-finger domain, including two additional CXXC motifs. The multi-stress resistant bacterium Deinococcus radiodurans encodes both Trx1 (DrTrx1) and Trx2 (DrTrx2), which act as members of the enzymatic antioxidant systems. In this study, we constructed Δdrtrx1 and Δdrtrx2 mutants and examined their survival rates under H2O2 treated conditions. Both drtrx1 and drtrx2 genes were induced following H2O2 treatment, and the Δdrtrx1 and Δdrtrx2 mutants showed a decrease in resistance toward H2O2, compared to the wild-type. Native DrTrx1 and DrTrx2 clearly displayed insulin and DTNB reduction activity, whereas mutant DrTrx1 and DrTrx2, which harbors the substitution of conserved cysteine to serine in its active site CXXC motif, showed almost no reduction activity. Mutations in the zinc binding cysteines did not fully eliminate the reduction activities of DrTrx2. Furthermore, we solved the crystal structure of full-length DrTrx2 at 1.96 Å resolution. The N-terminal zinc-finger domain of Trx2 is thought to be involved in Trx-target interaction and, from our DrTrx2 structure, the orientation of the zinc-finger domain of DrTrx2 and its interdomain interaction, between the Trx-fold domain and the zinc-finger domain, is clearly distinguished from those of the other Trx2 structures.

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