Synthesis of Tacaribe virus polypeptides in an in vitro coupled transcription and translation system.
We have analyzed polypeptides synthesized in a coupled in vitro transcription and translation system in response to detergent-disrupted Tacaribe virus. Analysis of the major Tacaribe virus-specified product by two-dimensional polyacrylamide gel electrophoresis indicated that it had an isoelectric point similar to that of the Tacaribe nucleocapsid polypeptide N; however, the in vitro product had an approximate mol. wt. of 73 000, compared to a mol. wt. of 68 000 for the N protein. The 73 000 dalton product was found to yield proteolytic cleavage products with similar electrophoretic mobilities to those obtained from the virion P and N proteins. These results, as well as pulse-chase experiments in Tacaribe virus-infected cells, suggest that a 73 000 dalton polypeptide may be processed to yield the N polypeptide. The polypeptides synthesized in the coupled system depended on the amount and type of virus added; addition of purified Shark River (SR) virus, a member of the Patois group of bunyaviruses, resulted in synthesis of a polypeptide of mol. wt. 22 000 which corresponds to the SR nucleocapsid protein.
Boersma
D P
DP
Compans
R W
RW
D001116:Arenaviridae / Q000235:genetics*; D002474:Cell-Free System; D007526:Isoelectric Point; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000096:biosynthesis*
D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase