RNA-binding properties and RNA chaperone activity of human peroxiredoxin 1

2012 ◽  
Vol 425 (4) ◽  
pp. 730-734 ◽  
Author(s):  
Ji-Hee Kim ◽  
Jeong-Mi Lee ◽  
Hae Na Lee ◽  
Eun-Kyung Kim ◽  
Bin Ha ◽  
...  
2007 ◽  
Vol 35 (4) ◽  
pp. 1257-1269 ◽  
Author(s):  
O. Mayer ◽  
L. Rajkowitsch ◽  
C. Lorenz ◽  
R. Konrat ◽  
R. Schroeder

2009 ◽  
Vol 84 (4) ◽  
pp. 2169-2175 ◽  
Author(s):  
Sonia Zúñiga ◽  
Jazmina L. G. Cruz ◽  
Isabel Sola ◽  
Pedro A. Mateos-Gómez ◽  
Lorena Palacio ◽  
...  

ABSTRACT Purified nucleocapsid protein (N protein) from transmissible gastroenteritis virus (TGEV) enhanced hammerhead ribozyme self-cleavage and favored nucleic acid annealing, properties that define RNA chaperones, as previously reported. Several TGEV N-protein deletion mutants were expressed in Escherichia coli and purified, and their RNA binding ability and RNA chaperone activity were evaluated. The smallest N-protein domain analyzed with RNA chaperone activity, facilitating DNA and RNA annealing, contained the central unstructured region (amino acids 117 to 268). Interestingly, N protein and its deletion mutants with RNA chaperone activity enhanced template switching in a retrovirus-derived heterologous system, reinforcing the concept that TGEV N protein is an RNA chaperone that could be involved in template switching. This result is in agreement with the observation that in vivo, N protein is not necessary for TGEV replication, but it is required for efficient transcription.


FEBS Letters ◽  
2011 ◽  
Vol 585 (16) ◽  
pp. 2575-2581 ◽  
Author(s):  
Wen-Li Pong ◽  
Zhi-Shun Huang ◽  
Pak-Guan Teoh ◽  
Chung-Chun Wang ◽  
Huey-Nan Wu

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