GATA zinc finger domain‐containing protein 2A ( GATAD2A ) deficiency reactivates fetal haemoglobin in patients with β‐thalassaemia through impaired formation of methyl‐binding domain protein 2 (MBD2)‐containing nucleosome remodelling and deacetylation (NuRD) complex

2021 ◽  
Author(s):  
Yunhao Liang ◽  
Xinhua Zhang ◽  
Yongqiong Liu ◽  
Liren Wang ◽  
Yuhua Ye ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Binding Domain ◽  
Zinc Finger Domain ◽  
Nurd Complex ◽  
Fetal Haemoglobin ◽  
Domain Protein

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 structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains

2009 ◽  
Vol 106 (17) ◽  
pp. 6933-6938 ◽  
Author(s):  
Ilaria Baglivo ◽  
Luigi Russo ◽  
Sabrina Esposito ◽  
Gaetano Malgieri ◽  
Mario Renda ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Coordination Sphere ◽  
Zinc Ion ◽  
Binding Domain ◽  
Hydrophobic Core ◽  
Zinc Finger Domain ◽  
High Sequence Identity ◽  
Zinc Coordination ◽  
Zinc Finger Domains

The recent characterization of the prokaryotic Cys2His2 zinc-finger domain, identified in Ros protein from Agrobacterium tumefaciens, has demonstrated that, although possessing a similar zinc coordination sphere, this domain is structurally very different from its eukaryotic counterpart. A search in the databases has identified ≈300 homologues with a high sequence identity to the Ros protein, including the amino acids that form the extensive hydrophobic core in Ros. Surprisingly, the Cys2His2 zinc coordination sphere is generally poorly conserved in the Ros homologues, raising the question of whether the zinc ion is always preserved in these proteins. Here, we present a functional and structural study of a point mutant of Ros protein, Ros56–142C82D, in which the second coordinating cysteine is replaced by an aspartate, 5 previously-uncharacterized representative Ros homologues from Mesorhizobium loti, and 2 mutants of the homologues. Our results indicate that the prokaryotic zinc-finger domain, which in Ros protein tetrahedrally coordinates Zn(II) through the typical Cys2His2 coordination, in Ros homologues can either exploit a CysAspHis2 coordination sphere, previously never described in DNA binding zinc finger domains to our knowledge, or lose the metal, while still preserving the DNA-binding activity. We demonstrate that this class of prokaryotic zinc-finger domains is structurally very adaptable, and surprisingly single mutations can transform a zinc-binding domain into a nonzinc-binding domain and vice versa, without affecting the DNA-binding ability. In light of our findings an evolutionary link between the prokaryotic and eukaryotic zinc-finger domains, based on bacteria-to-eukaryota horizontal gene transfer, is discussed.

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 Autographa californica Multiple Nucleopolyhedrovirus AC83 is a Per Os Infectivity Factor (PIF) Protein Required for Occlusion-Derived Virus (ODV) and Budded Virus Nucleocapsid Assembly as well as Assembly of the PIF Complex in ODV Envelopes

2016 ◽  
Vol 91 (5) ◽  
Author(s):  
Muhammad Afzal Javed ◽  
Siddhartha Biswas ◽  
Leslie G. Willis ◽  
Stephanie Harris ◽  
Caitlin Pritchard ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Core Gene ◽  
Infection Process ◽  
Binding Domain ◽  
Autographa Californica ◽  
Zinc Finger Domain ◽  
Chitin Binding Domain ◽  
New Model ◽  
Multiple Nucleopolyhedrovirus ◽  
Autographa Californica Multiple Nucleopolyhedrovirus

ABSTRACT Baculovirus occlusion-derived virus (ODV) initiates infection of lepidopteran larval hosts by binding to the midgut epithelia, which is mediated by per os infectivity factors (PIFs). Autographa californica multiple nucleopolyhedrovirus (AcMNPV) encodes seven PIF proteins, of which PIF1 to PIF4 form a core complex in ODV envelopes to which PIF0 and PIF6 loosely associate. Deletion of any pif gene results in ODV being unable to bind or enter midgut cells. AC83 also associates with the PIF complex, and this study further analyzed its role in oral infectivity to determine if it is a PIF protein. It had been proposed that AC83 possesses a chitin binding domain that enables transit through the peritrophic matrix; however, no chitin binding activity has ever been demonstrated. AC83 has been reported to be found only in the ODV envelopes, but in contrast, the Orgyia pseudotsugata MNPV AC83 homolog is associated with both ODV nucleocapsids and envelopes. In addition, unlike known pif genes, deletion of ac83 eliminates nucleocapsid formation. We propose a new model for AC83 function and show AC83 is associated with both ODV nucleocapsids and envelopes. We also further define the domain required for nucleocapsid assembly. The cysteine-rich region of AC83 is also shown not to be a chitin binding domain but a zinc finger domain required for the recruitment or assembly of the PIF complex to ODV envelopes. As such, AC83 has all the properties of a PIF protein and should be considered PIF8. In addition, pif7 (ac110) is reported as the 38th baculovirus core gene. IMPORTANCE ODV is essential for the per os infectivity of the baculovirus AcMNPV. To initiate infection, ODV binds to microvilli of lepidopteran midgut cells, a process which requires a group of seven virion envelope proteins called PIFs. In this study, we reexamined the function of AC83, a protein that copurifies with the ODV PIFs, to determine its role in the oral infection process. A zinc finger domain was identified and a new model for AC83 function was proposed. In contrast to previous studies, AC83 was found to be physically located in both the envelope and nucleocapsid of ODV. By deletion analysis, the AC83 domain required for nucleocapsid assembly was more finely delineated. We show that AC83 is required for PIF complex formation and conclude that it is a true per os infectivity factor and should be called PIF8.

scholarly journals An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex

2015 ◽  
Vol 43 (6) ◽  
pp. 3100-3113 ◽  
Author(s):  
Megha A. Desai ◽  
Heather D. Webb ◽  
Leander M. Sinanan ◽  
J. Neel Scarsdale ◽  
Ninad M. Walavalkar ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Binding Domain ◽  
Nurd Complex ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Region ◽  
Domain Protein

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 In vitro analysis of the zinc-finger motif in human replication protein A

1999 ◽  
Vol 337 (2) ◽  
pp. 311-317 ◽  
Author(s):  
Jiaowang DONG ◽  
Jang-Su PARK ◽  
Suk-Hee LEE
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Dna Polymerase ◽  
Protein A ◽  
Replication Protein A ◽  
Binding Domain ◽  
Replication Protein ◽  
Zinc Finger Motif ◽  
Zinc Finger Domain ◽  
Single Stranded Dna

Human replication protein A (RPA) is composed of 70, 34 and 11 kDa subunits (p70, p34 and p11 respectively) and functions in all three major DNA metabolic processes: replication, repair and recombination. Recent deletion analysis demonstrated that the large subunit of RPA, p70, has multiple functional domains, including a DNA polymerase α-stimulation domain and a single-stranded DNA-binding domain. It also contains a putative metal-binding domain of the 4-cysteine type (Cys-Xaa4-Cys-Xaa13-Cys-Xaa2-Cys) that is highly conserved among eukaryotes. To study the role of this domain in DNA metabolism, we created various p70 mutants that lack the zinc-finger motif (by Cys → Ala substitutions). Mutation at the zinc-finger domain (ZFM) abolished RPA's function in nucleotide excision repair (NER), but had very little impact on DNA replication. The failure of zinc-finger mutant RPA in NER may be explained by the observation that wild-type RPA significantly stimulated DNA polymerase δ activity, whereas only marginal stimulation was observed with zinc-finger mutant RPA. We also observed that ZFM reduced RPA's single-stranded DNA-binding activity by 2–3-fold in the presence of low amounts of RPA. Interestingly, the ZFM abolished phosphorylation of the p34 subunit by DNA-dependent protein kinase, but not that by cyclin-dependent kinase. Taker together, our results strongly suggest a positive role for RPA's zinc finger domain in its function.

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