NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein

ChemBioChem ◽  
2003 ◽  
Vol 4 (2-3) ◽  
pp. 171-180 ◽  
Author(s):  
Carla Isernia ◽  
Enrico Bucci ◽  
Marilisa Leone ◽  
Laura Zaccaro ◽  
Paola Di Lello ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Nmr Structure ◽  
Zinc Finger Domain

Cover Picture: NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein (ChemBioChem 2-3/2003)

ChemBioChem ◽  
2003 ◽  
Vol 4 (2-3) ◽  
pp. 125-125
Author(s):  
Carla Isernia ◽  
Enrico Bucci ◽  
Marilisa Leone ◽  
Laura Zaccaro ◽  
Paola Di Lello ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Nmr Structure ◽  
Zinc Finger Domain

The DnaJ-like zinc finger domain protein ORANGE localizes to the nucleus in etiolated cotyledons of Arabidopsis thaliana

PROTOPLASMA ◽  
2015 ◽  
Vol 253 (6) ◽  
pp. 1599-1604 ◽  
Author(s):  
Tian-Hu Sun ◽  
Fei Zhou ◽  
Chuan-Jun Liu ◽  
Zhong Zhuang ◽  
Shan Lu
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Domain Protein

scholarly journals NMR structure of the mengovirus Leader protein zinc-finger domain

FEBS Letters ◽  
2008 ◽  
Vol 582 (6) ◽  
pp. 896-900 ◽  
Author(s):  
Claudia C. Cornilescu ◽  
Frederick W. Porter ◽  
Kate Qin Zhao ◽  
Ann C. Palmenberg ◽  
John L. Markley
Keyword(s):  
Zinc Finger ◽  
Nmr Structure ◽  
Zinc Finger Domain ◽  
Leader Protein

scholarly journals The topoisomerase 3α zinc-finger domain T1 of Arabidopsis thaliana is required for targeting the enzyme activity to Holliday junction-like DNA repair intermediates

PLoS Genetics ◽  
2018 ◽  
Vol 14 (9) ◽  
pp. e1007674 ◽  
Author(s):  
Annika Dorn ◽  
Sarah Röhrig ◽  
Kristin Papp ◽  
Susan Schröpfer ◽  
Frank Hartung ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Dna Repair ◽  
Enzyme Activity ◽  
Zinc Finger ◽  
Holliday Junction ◽  
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 Arabidopsis MORC proteins function in the efficient establishment of RNA directed DNA methylation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yan Xue ◽  
Zhenhui Zhong ◽  
C. Jake Harris ◽  
Javier Gallego-Bartolomé ◽  
Ming Wang ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Arabidopsis Thaliana ◽  
Transposable Element ◽  
Zinc Finger ◽  
Protein Function ◽  
C Elegans ◽  
Eukaryotic Organisms

AbstractThe Microrchidia (MORC) family of ATPases are required for transposable element (TE) silencing and heterochromatin condensation in plants and animals, and C. elegans MORC-1 has been shown to topologically entrap and condense DNA. In Arabidopsis thaliana, mutation of MORCs has been shown to reactivate silent methylated genes and transposons and to decondense heterochromatic chromocenters, despite only minor changes in the maintenance of DNA methylation. Here we provide the first evidence localizing Arabidopsis MORC proteins to specific regions of chromatin and find that MORC4 and MORC7 are closely co-localized with sites of RNA-directed DNA methylation (RdDM). We further show that MORC7, when tethered to DNA by an artificial zinc finger, can facilitate the establishment of RdDM. Finally, we show that MORCs are required for the efficient RdDM mediated establishment of DNA methylation and silencing of a newly integrated FWA transgene, even though morc mutations have no effect on the maintenance of preexisting methylation at the endogenous FWA gene. We propose that MORCs function as a molecular tether in RdDM complexes to reinforce RdDM activity for methylation establishment. These findings have implications for MORC protein function in a variety of other eukaryotic organisms.

NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana

2016 ◽  
Vol 1864 (12) ◽  
pp. 1739-1747 ◽  
Author(s):  
Reza Omidvar ◽  
Youlin Xia ◽  
Fernando Porcelli ◽  
Holger Bohlmann ◽  
Gianluigi Veglia
Keyword(s):  
Arabidopsis Thaliana ◽  
Conformational Dynamics ◽  
Nmr Structure
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