scholarly journals Structural and biochemical characterization of HP0315 from Helicobacter pylori as a VapD protein with an endoribonuclease activity

2012 ◽  
Vol 40 (9) ◽  
pp. 4216-4228 ◽  
Author(s):  
Ae-Ran Kwon ◽  
Ji-Hun Kim ◽  
Sung Jean Park ◽  
Ki-Young Lee ◽  
Yu-Hong Min ◽  
...  
2004 ◽  
Vol 3 (8) ◽  
pp. 809-819 ◽  
Author(s):  
Laurent Terradot ◽  
Nathan Durnell ◽  
Min Li ◽  
Ming Li ◽  
Jeremiah Ory ◽  
...  

2010 ◽  
Vol 192 (9) ◽  
pp. 739-746 ◽  
Author(s):  
Mon-Juan Lee ◽  
Liu Chien-Liang ◽  
Ju-Ying Tsai ◽  
Wae-Ting Sue ◽  
Wan-Shun Hsia ◽  
...  

2004 ◽  
Vol 78 (22) ◽  
pp. 12218-12224 ◽  
Author(s):  
Kanchan Bhardwaj ◽  
Linda Guarino ◽  
C. Cheng Kao

ABSTRACT Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5′ of uridylates of RNAs. Blocking either the 5′ or 3′ terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn2+ at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg2+ and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn2+ needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.


2018 ◽  
Vol 308 (4) ◽  
pp. 425-437 ◽  
Author(s):  
Simon H. Bats ◽  
Célia Bergé ◽  
Nina Coombs ◽  
Laurent Terradot ◽  
Christine Josenhans

PLoS ONE ◽  
2019 ◽  
Vol 14 (6) ◽  
pp. e0218474 ◽  
Author(s):  
Sven Holtrup ◽  
Thomas Heimerl ◽  
Uwe Linne ◽  
Florian Altegoer ◽  
Frank Noll ◽  
...  

Author(s):  
A.M. Turgimbaeva ◽  
◽  
S.K. Abeldenov ◽  
M.K. Saparbayev ◽  
Y.M. Ramankulov ◽  
...  

2009 ◽  
Vol 83 (11) ◽  
pp. 5671-5682 ◽  
Author(s):  
Danny D. Nedialkova ◽  
Rachel Ulferts ◽  
Erwin van den Born ◽  
Chris Lauber ◽  
Alexander E. Gorbalenya ◽  
...  

ABSTRACT Nidoviruses (arteriviruses, coronaviruses, and roniviruses) are a phylogenetically compact but diverse group of positive-strand RNA viruses that includes important human and animal pathogens. Nidovirus RNA synthesis is mediated by a cytoplasmic membrane-associated replication/transcription complex that includes up to 16 viral nonstructural proteins (nsps), which carry common enzymatic activities, like the viral RNA polymerase, but also unusual and poorly understood RNA-processing functions. Of these, a conserved endoribonuclease (NendoU) is a major genetic marker that is unique to nidoviruses. NendoU activity was previously verified in vitro for the coronavirus nsp15, but not for any of its distantly related orthologs from other nidovirus lineages, like the arterivirus nsp11. Here, we show that the bacterially expressed nsp11 proteins of two arteriviruses, equine arteritis virus and porcine respiratory and reproductive syndrome virus, possess pyrimidine-specific endoribonuclease activity. RNA cleavage was independent of divalent cations in vitro and was greatly reduced by replacement of residues previously implicated in catalysis. Comparative characterization of the NendoU activity in arteriviruses and severe acute respiratory syndrome coronavirus revealed common and distinct features of their substrate requirements and reaction mechanism. Our data provide the first biochemical evidence of endoribonuclease activity associated with arterivirus nsp11 and support the conclusion that this remarkable RNA-processing enzyme, whose substrate in the infected cell remains to be identified, distinguishes nidoviruses from all other RNA viruses.


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