scholarly journals The maize ZmMIEL1 E3 ligase and ZmMYB83 transcription factor proteins interact and regulate the hypersensitive defence response

2021 ◽  
Author(s):  
Shailesh Karre ◽  
Saet‐Byul Kim ◽  
Rozalynne Samira ◽  
Peter Balint‐Kurti
Keyword(s):  
Transcription Factor ◽  
E3 Ligase ◽  
Defence Response ◽  
Transcription Factor Proteins

scholarly journals Divergent Roles of a Pair of Homologous Jumonji/Zinc-Finger–Class Transcription Factor Proteins in the Regulation of Arabidopsis Flowering Time

2004 ◽  
Vol 16 (10) ◽  
pp. 2601-2613 ◽  
Author(s):  
Bosl Noh ◽  
Seung-Hee Lee ◽  
Hyun-Jin Kim ◽  
Gibum Yi ◽  
Eun-Ah Shin ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Flowering Time ◽  
Zinc Finger ◽  
Transcription Factor Proteins

scholarly journals Intermolecular epistasis shaped the function and evolution of an ancient transcription factor and its DNA binding sites

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Dave W Anderson ◽  
Alesia N McKeown ◽  
Joseph W Thornton
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Sites ◽  
Steroid Hormone Receptor ◽  
Biological Processes ◽  
Epistatic Interactions ◽  
Dna Binding Sites ◽  
Evolutionary Paths ◽  
Historical Transition ◽  
Transcription Factor Proteins

Complexes of specifically interacting molecules, such as transcription factor proteins (TFs) and the DNA response elements (REs) they recognize, control most biological processes, but little is known concerning the functional and evolutionary effects of epistatic interactions across molecular interfaces. We experimentally characterized all combinations of genotypes in the joint protein-DNA sequence space defined by an historical transition in TF-RE specificity that occurred some 500 million years ago in the DNA-binding domain of an ancient steroid hormone receptor. We found that rampant epistasis within and between the two molecules was essential to specific TF-RE recognition and to the evolution of a novel TF-RE complex with unique derived specificity. Permissive and restrictive epistatic mutations across the TF-RE interface opened and closed potential evolutionary paths accessible by the other, making the evolution of each molecule contingent on its partner's history and allowing a molecular complex with novel specificity to evolve.

scholarly journals Inhibition of Vpx-Mediated SAMHD1 and Vpr-Mediated Host Helicase Transcription Factor Degradation by Selective Disruption of Viral CRL4 (DCAF1) E3 Ubiquitin Ligase Assembly

2017 ◽  
Vol 91 (9) ◽  
Author(s):  
Hong Wang ◽  
Haoran Guo ◽  
Jiaming Su ◽  
Yajuan Rui ◽  
Wenwen Zheng ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Transcription Factor ◽  
Drug Development ◽  
E3 Ligase ◽  
Zinc Binding ◽  
Binding Motif ◽  
Accessory Proteins ◽  
Immunodeficiency Virus ◽  
Zinc Coordination ◽  
Zinc Binding Motif

ABSTRACT The lentiviral accessory proteins Vpx and Vpr are known to utilize CRL4 (DCAF1) E3 ligase to induce the degradation of the host restriction factor SAMHD1 or host helicase transcription factor (HLTF), respectively. Selective disruption of viral CRL4 (DCAF1) E3 ligase could be a promising antiviral strategy. Recently, we have determined that posttranslational modification (neddylation) of Cullin-4 is required for the activation of Vpx-CRL4 (DCAF1) E3 ligase. However, the mechanism of Vpx/Vpr-CRL4 (DCAF1) E3 ligase assembly is still poorly understood. Here, we report that zinc coordination is an important regulator of Vpx-CRL4 E3 ligase assembly. Residues in a conserved zinc-binding motif of Vpx were essential for the recruitment of the CRL4 (DCAF1) E3 complex and Vpx-induced SAMHD1 degradation. Importantly, altering the intracellular zinc concentration by treatment with the zinc chelator N,N,N′-tetrakis-(2′-pyridylmethyl)ethylenediamine (TPEN) potently blocked Vpx-mediated SAMHD1 degradation and inhibited wild-type SIVmac (simian immunodeficiency virus of macaques) infection of myeloid cells, even in the presence of Vpx. TPEN selectively inhibited Vpx and DCAF1 binding but not the Vpx-SAMHD1 interaction or Vpx virion packaging. Moreover, we have shown that zinc coordination is also important for the assembly of the HIV-1 Vpr-CRL4 E3 ligase. In particular, Vpr zinc-binding motif mutation or TPEN treatment efficiently inhibited Vpr-CRL4 (DCAF1) E3 ligase assembly and Vpr-mediated HLTF degradation or Vpr-induced G2 cell cycle arrest. Collectively, our study sheds light on a conserved strategy by the viral proteins Vpx and Vpr to recruit host CRL4 (DCAF1) E3 ligase, which represents a target for novel anti-human immunodeficiency virus (HIV) drug development. IMPORTANCE The Vpr and its paralog Vpx are accessory proteins encoded by different human immunodeficiency virus (HIV)/simian immunodeficiency virus (SIV) lentiviruses. To facilitate viral replication, Vpx has evolved to induce SAMHD1 degradation and Vpr to mediate HLTF degradation. Both Vpx and Vpr perform their functions by recruiting CRL4 (DCAF1) E3 ligase. In this study, we demonstrate that the assembly of the Vpx- or Vpr-CRL4 E3 ligase requires a highly conserved zinc-binding motif. This motif is specifically required for the DCAF1 interaction but not for the interaction of Vpx or Vpr with its substrate. Selective disruption of Vpx- or Vpr-CRL4 E3 ligase function was achieved by zinc sequestration using N,N,N′-tetrakis-(2′-pyridylmethyl)ethylenediamine (TPEN). At the same time, zinc sequestration had no effect on zinc-dependent cellular protein functions. Therefore, information obtained from this study may be important for novel anti-HIV drug development.

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