About: Efficient Autoproteolytic Processing of the MHV-A59 3C-like Proteinase from the Flanking Hydrophobic Domains Requires Membranes

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About: Efficient Autoproteolytic Processing of the MHV-A59 3C-like Proteinase from the Flanking Hydrophobic Domains Requires Membranes Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Efficient Autoproteolytic Processing of the MHV-A59 3C-like Proteinase from the Flanking Hydrophobic Domains Requires Membranes
Creator	Weiss, Susan Bonilla, Pedro Khan, Farah Mayreddy, Ravi Piñ Ó N, Josefina Turner, Julie
Source	Elsevier; Medline; PMC
abstract	Abstract The replicase gene of the coronavirus MHV-A59 encodes a serine-like proteinase similar to the 3C proteinases of picornaviruses. This proteinase domain is flanked on both sides by hydrophobic, potentially membrane-spanning, regions. Cell-free expression of a plasmid encoding only the 3C-like proteinase (3CLpro) resulted in the synthesis of a 29-kDa protein that was specifically recognized by an antibody directed against the carboxy-terminal region of the proteinase. A protein of identical mobility was detected in MHV-A59-infected cell lysates.In vitroexpression of a plasmid encoding the 3CLpro and portions of the two flanking hydrophobic regions resulted in inefficient processing of the 29-kDa protein. However, the efficiency of this processing event was enhanced by the addition of canine pancreatic microsomes to the translation reaction, or removal of one of the flanking hydrophobic domains. Proteolysis was inhibited in the presence ofN-ethylmaleimide (NEM) or by mutagenesis of the catalytic cysteine residue of the proteinase, indicating that the 3CLpro is responsible for its autoproteolytic cleavage from the flanking domains. Microsomal membranes were unable to enhance thetransprocessing of a precursor containing the inactive proteinase domain and both hydrophobic regions by a recombinant 3CLpro expressed fromEscherichia coli.Membrane association assays demonstrated that the 29-kDa 3CLpro was present in the soluble fraction of the reticulocyte lysates, while polypeptides containing the hydrophobic domains associated with the membrane pellets. With the help of a viral epitope tag, we identified a 22-kDa membrane-associated polypeptide as the proteolytic product containing the amino-terminal hydrophobic domain.
has issue date	1997-04-14(xsd:dateTime)
bibo:doi	10.1006/viro.1997.8503
bibo:pmid	9143287
has license	els-covid
sha1sum (hex)	ae26337e6fe2ba4e94f90b8884854b18eabb6dfe
schema:url	https://doi.org/10.1006/viro.1997.8503
resource representing a document's title	Efficient Autoproteolytic Processing of the MHV-A59 3C-like Proteinase from the Flanking Hydrophobic Domains Requires Membranes
has PubMed Central identifier	PMC7130731
has PubMed identifier	9143287
schema:publication	Virology
resource representing a document's body	covid:ae26337e6fe2ba4e94f90b8884854b18eabb6dfe#body_text
is schema:about of	named entity 'EFFICIENT' named entity 'MEMBRANES' named entity 'processing' named entity 'identical' named entity 'hydrophobic' named entity 'proteinase' named entity 'In vitro' named entity 'presence' named entity 'encodes' named entity 'enhanced' named entity 'Hydrophobic' named entity 'FLANKING' named entity 'DEMONSTRATED' named entity 'RECOMBINANT' named entity 'PICORNAVIRUSES' named entity 'MOBILITY' named entity 'CORONAVIRUS' named entity 'TRANSLATION' named entity 'EXPRESSED' named entity 'EPITOPE TAG' named entity 'PREDICTED' named entity 'EXPRESSION' named entity 'REPLICASE' named entity 'POLYPEPTIDE' named entity 'REMOVAL' named entity 'ASSOCIATION' named entity 'CYSTEINE RESIDUE' named entity 'PROTEIN' named entity 'TERMINAL' named entity 'PROTEOLYTIC' named entity 'PRESENCE OF' named entity 'INACTIVE' named entity 'N-ETHYLMALEIMIDE' named entity 'HELP' named entity 'MICROSOMAL' named entity 'FREE' named entity 'ONE OF' named entity 'SERINE' named entity 'FLANKED' named entity 'LIKE' named entity 'IDENTICAL' named entity 'PRECURSOR' named entity 'CARBOXY' named entity 'ITS' named entity 'IN VITRO' named entity 'VIRAL' named entity 'HYDROPHOBIC' named entity 'A59' named entity 'PROCESSING' named entity 'PROTEINASE' named entity 'LIKE' named entity 'INHIBITED' named entity 'FLANKING' named entity 'MICROSOMES' named entity 'PROTEIN ' named entity 'REGIONS' named entity 'MEMBRANE' named entity 'RETICULOCYTE' named entity 'CATALYTIC' named entity 'CELL' named entity 'PELLETS' named entity 'PRODUCT' named entity 'PROTEINASE' named entity 'CONTAINING' named entity 'ENHANCED' named entity 'MHV' named entity 'MUTAGENESIS' named entity 'INEFFICIENT' named entity '1997' named entity 'INDICATING' named entity 'PANCREATIC' named entity 'ASSOCIATED WITH' named entity 'INFECTED CELL' named entity 'SOLUBLE FRACTION' named entity 'FLANK' named entity 'MHV'

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