Overview:

Coronaviruses codes for a bifunctional non-structural protein 14 (NSP14) that is important for viral replication and transcription. NSP14 contains an N-terminal exo-ribonuclease (ExoN) domain for proof reading during viral replication and a C-terminal N-7 methyltransferase (N7-MTase) domain for mRNA capping. NSP14 associates with several viral proteins (1). It can bind to NSP10 and the resulting complex exhibits enhanced ExoN activity in vitro (2). It can also bind to the polymerase complex (NSP12/NSP8/NSP7) forming a complex that retains all associated enzymatic activities (3).

Gene Aliases:

NSP14: Non-structural protein 14

Genebank Number:

QHD43415

Formulation:

Recombinant protein stored in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.25mM DTT, 25% glycerol.

References:

1. Ma, Y. et al: Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. PNAS, USA. (2015), 112(30):9436–9441.

2. Bouvet, M. et al: RNA 3′-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc Natl Acad Sci USA. (2012), 109:9372–9377.

3. Subissi, L. et al: One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc Natl Acad Sci USA. (2014), 111:E3900–E3909.