scholarly journals Targeting Ligandable Pockets on Plant Homeodomain (PHD) Zinc Finger Domains by a Fragment-Based Approach

2018 ◽  
Vol 13 (4) ◽  
pp. 915-921 ◽  
Author(s):  
Anastasia Amato ◽  
Xavier Lucas ◽  
Alessio Bortoluzzi ◽  
David Wright ◽  
Alessio Ciulli
Keyword(s):  
Zinc Finger ◽  
Plant Homeodomain ◽  
Zinc Finger Domains

scholarly journals Determination of DNA binding specificities of mutated zinc finger domains

FEBS Letters ◽  
1991 ◽  
Vol 283 (1) ◽  
pp. 23-26 ◽  
Author(s):  
Hans-Jürgen Thiesen ◽  
Christian Bach
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Zinc Finger Domains

scholarly journals Biochemical Activities of Highly Purified, Catalytically Active Human APOBEC3G: Correlation with Antiviral Effect

2006 ◽  
Vol 80 (12) ◽  
pp. 5992-6002 ◽  
Author(s):  
Yasumasa Iwatani ◽  
Hiroaki Takeuchi ◽  
Klaus Strebel ◽  
Judith G. Levin
Keyword(s):  
Zinc Finger ◽  
Cytidine Deaminase ◽  
Antiviral Effect ◽  
Minimum Length ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Pure System ◽  
Dna And Rna ◽  
Catalytically Active ◽  
Zinc Finger Domains

ABSTRACT APOBEC3G (APO3G), a cytidine deaminase with two zinc finger domains, inhibits human immunodeficiency virus type 1 replication in the absence of Vif. Here, we provide a comprehensive molecular analysis of the deaminase and nucleic acid binding activities of human APO3G using a pure system containing only one protein component, i.e., highly purified, catalytically active enzyme expressed in a baculovirus system. We demonstrate that APO3G deaminates cytosines in single-stranded DNA (ssDNA) only, whereas it binds efficiently to ssDNA and ssRNA, about half as well to a DNA/RNA hybrid, and poorly to double-stranded DNA and RNA. In addition, the base specificities for deamination and binding of ssDNA are not correlated. The minimum length required for detection of APO3G binding to an ssDNA oligonucleotide in an electrophoretic mobility shift assay is 16 nucleotides. Interestingly, if nucleocapsid protein and APO3G are present in the same reaction, we find that they do not interfere with each other's binding to RNA and a complex containing the RNA and both proteins is formed. Finally, we also identify the functional activities of each zinc finger domain. Thus, although both zinc finger domains have the ability to bind nucleic acids, the first zinc finger contributes more to binding and APO3G encapsidation into virions than finger two. In contrast, deamination is associated exclusively with the second zinc finger. Moreover, zinc finger two is more important than finger one for the antiviral effect, demonstrating a correlation between deaminase and antiviral activities.

Structural Analyses of Zinc Finger Domains for Specific Interactions with DNA

2016 ◽  
Vol 26 (12) ◽  
pp. 2019-2029 ◽  
Author(s):  
Ki Seong Eom ◽  
Jin Sung Cheong ◽  
Seung Jae Lee
Keyword(s):  
Zinc Finger ◽  
Specific Interactions ◽  
Zinc Finger Domains

scholarly journals The zinc finger domains in U2AF26 and U2AF35 have diverse functionalities including a role in controlling translation

RNA Biology ◽  
2020 ◽  
Vol 17 (6) ◽  
pp. 843-856 ◽  
Author(s):  
Olga Herdt ◽  
Stefan Reich ◽  
Jan Medenbach ◽  
Bernd Timmermann ◽  
Didrik Olofsson ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Domains

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.

Sign in / Sign up

Export Citation Format

Share Document