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

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 The Arabidopsis a zinc finger domain protein ARS1 is essential for seed germination and ROS homeostasis in response to ABA and oxidative stress

2015 ◽  
Vol 6 ◽  
Author(s):  
Dongwon Baek ◽  
Joon-Yung Cha ◽  
Songhwa Kang ◽  
Bokyung Park ◽  
Hyo-Jung Lee ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Seed Germination ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Ros Homeostasis ◽  
Domain Protein ◽  
And Oxidative Stress

scholarly journals Author response: A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking

2015 ◽  
Author(s):  
Thomas Pohlmann ◽  
Sebastian Baumann ◽  
Carl Haag ◽  
Mario Albrecht ◽  
Michael Feldbrügge
Keyword(s):  
Zinc Finger ◽  
Author Response ◽  
Zinc Finger Domain ◽  
Mrna Transport ◽  
Endosome Trafficking ◽  
Domain Protein

scholarly journals The DnaJ-Like Zinc Finger Domain Protein PSA2 Affects Light Acclimation and Chloroplast Development in Arabidopsis thaliana

2016 ◽  
Vol 7 ◽  
Author(s):  
Yan-Wen Wang ◽  
Si-Ming Chen ◽  
Wei-Jie Wang ◽  
Xing-Qi Huang ◽  
Chang-Fang Zhou ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Zinc Finger ◽  
Chloroplast Development ◽  
Light Acclimation ◽  
Zinc Finger Domain ◽  
Domain Protein

scholarly journals Interactions of the Trypanosoma brucei brucei zinc-finger-domain protein ZC3H28

Parasitology ◽  
2021 ◽  
pp. 1-51
Author(s):  
Tania Bishola Tshitenge ◽  
Christine Clayton
Keyword(s):  
Trypanosoma Brucei ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Trypanosoma Brucei Brucei ◽  
Domain Protein

scholarly journals Snowy cotyledon 2: the identification of a zinc finger domain protein essential for chloroplast development in cotyledons but not in true leaves

2008 ◽  
Vol 66 (6) ◽  
pp. 599-608 ◽  
Author(s):  
Verónica Albrecht ◽  
Anke Ingenfeld ◽  
Klaus Apel
Keyword(s):  
Zinc Finger ◽  
Chloroplast Development ◽  
Zinc Finger Domain ◽  
Domain Protein

scholarly journals Bromodomain Adjacent to Zinc Finger Domain Protein 1A

2020 ◽  
Author(s):  
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Domain Protein

scholarly journals A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Thomas Pohlmann ◽  
Sebastian Baumann ◽  
Carl Haag ◽  
Mario Albrecht ◽  
Michael Feldbrügge
Keyword(s):  
Zinc Finger ◽  
Membrane Trafficking ◽  
Molecular Motors ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Detailed Knowledge ◽  
Zinc Finger Domain ◽  
Domain Protein ◽  
Dependent Transport

An emerging theme in cellular logistics is the close connection between mRNA and membrane trafficking. A prominent example is the microtubule-dependent transport of mRNAs and associated ribosomes on endosomes. This coordinated process is crucial for correct septin filamentation and efficient growth of polarised cells, such as fungal hyphae. Despite detailed knowledge on the key RNA-binding protein and the molecular motors involved, it is unclear how mRNAs are connected to membranes during transport. Here, we identify a novel factor containing a FYVE zinc finger domain for interaction with endosomal lipids and a new PAM2-like domain required for interaction with the MLLE domain of the key RNA-binding protein. Consistently, loss of this FYVE domain protein leads to specific defects in mRNA, ribosome, and septin transport without affecting general functions of endosomes or their movement. Hence, this is the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mRNPs to endosomes.

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