Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells
نویسندگان
چکیده
منابع مشابه
Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein.
Ribosome biogenesis in Saccharomyces cerevisiae occurs primarily in a specialized nuclear compartment termed the nucleolus within which the rRNA genes are transcribed by RNA polymerase I into a large 35 S rRNA precursor. The ensuing association/dissociation and catalytic activity of numerous trans-acting protein factors, RNAs and ribosomal proteins ultimately leads to the maturation of the prec...
متن کاملStructure of Semliki Forest virus core protein.
Alphaviruses are enveloped, insect-borne viruses, which contains a positive-sense RNA genome. The protein capsid is surrounded by a lipid membrane, which is penetrated by glycoprotein spikes. The structure of the Sindbis virus (SINV) (the type virus) core protein (SCP) was previously determined and found to have a chymotrypsin-like structure. SCP is a serine proteinase which cleaves itself from...
متن کاملSequential translation of nonstructural proteins in cells infected with a Semliki Forest virus mutant.
Four nonstructural proteins with apparent molecular weights of 70,000 (ns-70), 86,000 (ns-86), 78,000 (ns-78), and 60,000 (ns-60) were translated in cells infected with Semliki Forest virus ts-1 mutant and maintained at the restrictive temperature. After synchronization of the initiation of protein synthesis these proteins were synthesized in the above order, suggesting that they are translated...
متن کاملAction of brefeldin A on translation in Semliki Forest virus-infected HeLa cells and cells doubly infected with poliovirus.
Brefeldin A (BFA) is a macrolide antibiotic that blocks membrane traffic through the vesicular system and affects the glycosylation of viral glycoproteins. Treatment of HeLa cells infected with Semliki Forest virus (SFV) with BFA enhances the synthesis of late viral proteins. Proteolytic cleavage of p107 is partially blocked and viral glycoproteins accumulate in BFA-treated cells. This enhanced...
متن کاملQsr1p, a 60S ribosomal subunit protein, is required for joining of 40S and 60S subunits.
QSR1 is a recently discovered, essential Saccharomyces cerevisiae gene, which encodes a 60S ribosomal subunit protein. Thirty-one unique temperature-sensitive alleles of QSR1 were generated by regional codon randomization within a conserved 20-amino-acid sequence of the QSR1-encoded protein. The temperature-sensitive mutants arrest as viable, large, unbudded cells 24 to 48 h after a shift to 37...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1976
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.20.1.203-210.1976