Faculty Opinions recommendation of BORIS, a novel male germ-line-specific protein associated with epigenetic reprogramming events, shares the same 11-zinc-finger domain with CTCF, the insulator protein involved in reading imprinting marks in the soma.

2002 ◽  
Author(s):  
Anjana Rao
Keyword(s):  
Zinc Finger ◽  
Germ Line ◽  
Specific Protein ◽  
Epigenetic Reprogramming ◽  
Zinc Finger Domain ◽  
Male Germ Line ◽  
Insulator Protein

Effect of Silver Nanoparticles on SRC Activity in Male Germ-line Stem Cells

2006 ◽  
Author(s):  
Laura K. Braydich-Stolle ◽  
Saber Hussain ◽  
John J. Schlager ◽  
Marie-Claude Hofmann
Keyword(s):  
Stem Cells ◽  
Silver Nanoparticles ◽  
Germ Line ◽  
Male Germ Line

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

RADHA - a new male germ line-specific chromosomal protein of Drosophila

Chromosoma ◽  
1999 ◽  
Vol 108 (4) ◽  
pp. 235-242 ◽  
Author(s):  
Harry R. Harhangi ◽  
Xiaoping Sun ◽  
Ya Xian Wang ◽  
Anna Akhmanova ◽  
Koos Miedema ◽  
...  
Keyword(s):  
Germ Line ◽  
Chromosomal Protein ◽  
Male Germ Line
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