Literature DB >> 206439

Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme.

H R Pelham.   

Abstract

In contrast to other cell-free translation systems, the mRNA-dependent reticulocyte lysate can translate encephalomyocarditis virus RNA efficiently and completely when supplemented with heterologous tRNA. Cleavage of the nascent polypeptide chain occurs, and one of the translation products appears to be a specific proteolytic enzyme which correctly processes the primary products. The identity of the proteins made in vitro was verified by comparison with infected cell proteins on dodecylsulphate/polyacrylamide gels, and by mapping their coding sequences on the viral genome.

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Year:  1978        PMID： 206439     DOI： 10.1111/j.1432-1033.1978.tb12260.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  54 in total

1.  Translation of encephalomyocarditis virus RNA in reticulocyte lysates: kinetic analysis of the formation of virion proteins and a protein required for processing.

Authors:  D S Shih; C T Shih; D Zimmern; R R Rueckert; P Kaesberg
Journal:  J Virol       Date:  1979-05       Impact factor: 5.103

2.  Virus-specified protease in poliovirus-infected HeLa cells.

Authors:  B Korant; N Chow; M Lively; J Powers
Journal:  Proc Natl Acad Sci U S A       Date:  1979-06       Impact factor: 11.205

3.  Protease required for processing picornaviral coat protein resides in the viral replicase gene.

Authors:  A C Palmenberg; M A Pallansch; R R Rueckert
Journal:  J Virol       Date:  1979-12       Impact factor: 5.103

4.  Expression, purification, and properties of recombinant encephalomyocarditis virus RNA-dependent RNA polymerase.

Authors:  S Sankar; A G Porter
Journal:  J Virol       Date:  1991-06       Impact factor: 5.103

Review 5.  Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.

Authors:  W G Dougherty; B L Semler
Journal:  Microbiol Rev       Date:  1993-12

6.  Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity.

Authors:  P G Dewalt; M A Lawson; R J Colonno; B L Semler
Journal:  J Virol       Date:  1989-08       Impact factor: 5.103

7.  Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families.

Authors:  P Argos; G Kamer; M J Nicklin; E Wimmer
Journal:  Nucleic Acids Res       Date:  1984-09-25       Impact factor: 16.971

8.  Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells.

Authors:  L Tillotson; A J Shatkin
Journal:  J Virol       Date:  1992-04       Impact factor: 5.103

9.  Biochemical map of polypeptides specified by foot-and-mouth disease virus.

Authors:  M J Grubman; B H Robertson; D O Morgan; D M Moore; D Dowbenko
Journal:  J Virol       Date:  1984-05       Impact factor: 5.103

10.  The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region.

Authors:  A C Palmenberg; E M Kirby; M R Janda; N L Drake; G M Duke; K F Potratz; M S Collett
Journal:  Nucleic Acids Res       Date:  1984-03-26       Impact factor: 16.971
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