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

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 The zinc finger domain of IKKγ (NEMO) protein in health and disease

2010 ◽  
Vol 14 (10) ◽  
pp. 2404-2414 ◽  
Author(s):  
Amde Selassie Shifera
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Health And Disease

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

Fluorescence ‘reading-out’ of the molecular-recognition process

1992 ◽  
pp. 1341-1345 ◽  
Author(s):  
Izuo Aoki ◽  
Takaaki Harada ◽  
Toru Sakaki ◽  
Yohko Kawahara ◽  
Seiji Shinkai
Keyword(s):  
Molecular Recognition ◽  
Recognition Process ◽  
Fluorescence Reading

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
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