Structural domains of SARS-CoV-2 nucleocapsid protein coordinate to compact long nucleic acid substrates.

ABSTRACT: The SARS-CoV-2 nucleocapsid (N) protein performs several functions including binding, compacting, and packaging the ∼30 kb viral genome into the viral particle. N protein consists of two ordered domains, with the N terminal domain (NTD) primarily associated with RNA binding and the C terminal domain (CTD) primarily associated with dimerization/oligomerization, and three intrinsically disordered regions, an N-arm, a C-tail, and a linker that connects the NTD and CTD. We utilize an optical tweezers system to isolate a long single-stranded nucleic acid substrate to measure directly the binding and packaging function of N protein at a single molecule level in real time. We find that N protein binds the nucleic acid substrate with high affinity before oligomerizing and forming a highly compact

SUBMITTER: Morse M 

PROVIDER: S-EPMC9841419 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature