Tethering of proteins to RNAs using the bovine immunodeficiency virus–Tat peptide and BIV–TAR RNA

2012 ◽  
Vol 427 (2) ◽  
pp. 130-132 ◽  
Author(s):  
Motoaki Wakiyama ◽  
Yoko Kaitsu ◽  
Reiko Muramatsu ◽  
Koji Takimoto ◽  
Shigeyuki Yokoyama
2004 ◽  
Vol 78 (3) ◽  
pp. 1456-1463 ◽  
Author(s):  
Baode Xie ◽  
Valerie Calabro ◽  
Mark A. Wainberg ◽  
Alan D. Frankel

ABSTRACT The interaction between the arginine-rich motif (ARM) of the human immunodeficiency virus (HIV) Tat protein and TAR RNA is essential for Tat activation and viral replication. Two related lentiviruses, bovine immunodeficiency virus (BIV) and Jembrana disease virus (JDV), also require Tat ARM-TAR interactions to mediate activation, but the viruses have evolved different RNA-binding strategies. Interestingly, the JDV ARM can act as a “chameleon,” adopting both the HIV and BIV TAR binding modes. To examine how RNA-protein interactions may evolve in a viral context and possibly to identify peptides that recognize HIV TAR in novel ways, we devised a retroviral system based on HIV replication to amplify and select for RNA binders. We constructed a combinatorial peptide library based on the BIV Tat ARM and identified peptides that, like the JDV Tat ARM, also function through HIV TAR, revealing unexpected sequence characteristics of an RNA-binding chameleon. The results suggest that a retroviral screening approach may help identify high-affinity TAR binders and may provide new insights into the evolution of RNA-protein interactions.


Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 3096-3108 ◽  
Author(s):  
Mark A. Farrow ◽  
Fareed Aboul-ela ◽  
David Owen ◽  
Alexander Karpeisky ◽  
Leonid Beigelman ◽  
...  

1998 ◽  
Vol 63 (6) ◽  
pp. 842-850 ◽  
Author(s):  
Iwona Buskiewicz ◽  
Malgorzata Giel-Pietraszuk ◽  
Piotr Mucha ◽  
Piotr Rekowski ◽  
Gotfryd Kupryszewski ◽  
...  

We present data on the interaction of arginine-rich peptides of human immunodeficiency virus (HIV-Tat) with tRNAPhe of Saccharomyces cerevisiae. We have found that tRNA forms complexes with the Tat1 peptide of amino acid sequence GRKKRRQRRRA and its mutants where R is replaced by D-arginine, citrulline or ornithine. The structure of tRNA-Tat1 complex was probed by specific RNases digestions and Pb2+-induced cleavage of phosphodiester bond of guanosine. The nucleotide sequence UGGG located in the dihydrouridine loop of tRNAPhe binds to Tat peptide and therefore is specifically protected against RNases and is not hydrolyzed by Pb2+ ion. It seems that the peptide-RNA complex formation depends on direct recognition of guanine moieties of tRNA with arginine residues. These interactions are similar to those observed in many DNA-protein complexes, but are different from those previously observed for TAR RNA-Tat complexes.


2013 ◽  
Vol 44 (1) ◽  
pp. 21 ◽  
Author(s):  
Hong-yan Guo ◽  
Yong-gang Ma ◽  
Yuan-ming Gai ◽  
Zhi-bin Liang ◽  
Jing Ma ◽  
...  

2001 ◽  
Vol 20 (4-7) ◽  
pp. 441-449 ◽  
Author(s):  
Fabien Darfeuille ◽  
Christian Cazenave ◽  
Sergei Gryaznov ◽  
Frédéric Ducongé ◽  
Carmelo Di Primo ◽  
...  

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