In-vitro acetylation of SARS-CoV and SARS-CoV-2 nucleocapsid proteins by human PCAF and GCN5.
Biochem Biophys Res Commun
; 557: 273-279, 2021 06 11.
Article
in English
| MEDLINE | ID: covidwho-1174101
ABSTRACT
Recently, the novel coronavirus (SARS-CoV-2), which has spread from China to the world, was declared a global public health emergency, which causes lethal respiratory infections. Acetylation of several proteins plays essential roles in various biological processes, such as viral infections. We reported that the nucleoproteins of influenza virus and Zaire Ebolavirus were acetylated, suggesting that these modifications contributed to the molecular events involved in viral replication. Similar to influenza virus and Ebolavirus, the coronavirus also contains single-stranded RNA, as its viral genome interacts with the nucleocapsid (N) proteins. In this study, we report that SARS-CoV and SARS-CoV-2 N proteins are strongly acetylated by human histone acetyltransferases, P300/CBP-associated factor (PCAF), and general control nonderepressible 5 (GCN5), but not by CREB-binding protein (CBP) in vitro. Liquid chromatography-mass spectrometry analyses identified 2 and 12 acetyl-lysine residues from SARS-CoV and SARS-CoV-2 N proteins, respectively. Particularly in the SARS-CoV-2 N proteins, the acetyl-lysine residues were localized in or close to several functional sites, such as the RNA interaction domains and the M-protein interacting site. These results suggest that acetylation of SARS-CoV-2 N proteins plays crucial roles in their functions.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Severe Acute Respiratory Syndrome
/
Severe acute respiratory syndrome-related coronavirus
/
Histone Acetyltransferases
/
P300-CBP Transcription Factors
/
Coronavirus Nucleocapsid Proteins
/
SARS-CoV-2
/
COVID-19
Limits:
Humans
Language:
English
Journal:
Biochem Biophys Res Commun
Year:
2021
Document Type:
Article
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