EV71 3C protease induces apoptosis by cleavage of hnRNP A1 to promote apaf-1 translation

Coxsackievirus B3 protease 3C induces cell death in eukaryotic cells

Abstract: Coxsackievirus B3 (CVB3) is the most common agent known to cause viral myocarditis. The viral genome encodes a single polyprotein that is cleaved to produce several proteins by virally encoded proteases. Most of this proteolytic processing is catalyzed by a cysteine protease called 3C. The 3C protease plays major role in viral replication and cellular damage. To understand the mecha...

Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells.

Infection of cells by foot-and-mouth disease virus (FMDV) results in the rapid inhibition of host cell protein synthesis. This process is accompanied by the early cleavage of the translation initiation factor eIF4G, a component of the cap-binding complex eIF4F. This cleavage is mediated by the leader (L) protease. Subsequently, as the virus proteins accumulate, secondary cleavages of eIF4G occu...

Factors eIF4A and eIF4G within Infected Induces Cleavage of Translation Initiation Foot-and-Mouth Disease Virus 3C Protease

APAF 1 ( Apoptotic protease activating factor 1 )

Five isoforms of APAF1 cDNA have been identified in Homo sapiens: The original APAF1 (also called Apaf-1S) is 3585 bp long (it contains 12 WD40 repeats); The APAF1-1M isoform (3618 bp) contains an insertion of 33 nt after position 295 of the first published sequence (11 aa insertion GKDSVSGITSY between aa 98 and 99; it also contains 12 WD40 repeats); The APAF1XS isoform (3516 bp) contains the s...

PRMT5 regulates IRES-dependent translation via methylation of hnRNP A1

The type II arginine methyltransferase PRMT5 is responsible for the symmetric dimethylation of histone to generate the H3R8me2s and H4R3me2s marks, which correlate with the repression of transcription. However, the protein level of a number of genes (MEP50, CCND1, MYC, HIF1a, MTIF and CDKN1B) are reported to be downregulated by the loss of PRMT5, while their mRNA levels remain unchanged, which ...