Author: Adedeji, Adeyemi O.; Marchand, Bruno; te Velthuis, Aartjan J. W.; Snijder, Eric J.; Weiss, Susan; Eoff, Robert L.; Singh, Kamalendra; Sarafianos, Stefan G.
Title: Mechanism of Nucleic Acid Unwinding by SARS-CoV Helicase Document date: 2012_5_15
ID: 1ssh296a_26
Snippet: Our data suggest that nsp12 and nsp13 are in contact during viral replication, and are consistent with previous yeast two hybrid system studies, which have shown that these two proteins can physically interact with each other [31] . The enhancement of nsp13 activity in the presence of nsp12 is specific as it does not occur in the presence of another RdRp, such as FMDV 3Dpol. Moreover, it was observed not only for GST-nsp13, but also for the H 6 -.....
Document: Our data suggest that nsp12 and nsp13 are in contact during viral replication, and are consistent with previous yeast two hybrid system studies, which have shown that these two proteins can physically interact with each other [31] . The enhancement of nsp13 activity in the presence of nsp12 is specific as it does not occur in the presence of another RdRp, such as FMDV 3Dpol. Moreover, it was observed not only for GST-nsp13, but also for the H 6 -nsp13 ( Figures 6C and 6D ) and MBP-nsp13 (data not shown), demonstrating that it is not an artifact of the fusion tag. To our knowledge, this is the first report of a nidovirus RNA helicase activity enhancement by an RdRp. The synergy between the two enzymes is likely to be important for coronavirus replication, as is the case in other bacterial, mitochondrial, bacteriophage DNA-or viral RNA-replication systems. In these cases, the DNA polymerase [49, 51, 57, 58, 59] or the RNA polymerase [60] were reported to enhance unwinding by the corresponding helicase.
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