Antisense RNA has emerged as a crucial regulator of opposite-strand 
protein-coding genes in the long noncoding RNA (lncRNA) category, but little is 
known about their dynamics and decay process in the context of a stress 
response. Antisense transcripts from the fission yeast fbp1 locus (fbp1-as) are 
expressed in glucose-rich conditions and anticorrelated with transcription of 
metabolic stress-induced lncRNA (mlonRNA) and mRNA on the sense strand during 
glucose starvation. Here, we investigate the localization and decay of antisense 
RNAs at fbp1 and other loci, and propose a model to explain the rapid switch 
between antisense and sense mlonRNA/mRNA transcription triggered by glucose 
starvation. We show that fbp1-as shares many features with mRNAs, such as a 
5'-cap and poly(A)-tail, and that its decay partially depends upon Rrp6, a 
cofactor of the nuclear exosome complex involved in 3'-5' degradation of RNA. 
Fluorescence in situ hybridization and polysome fractionation show that the 
majority of remaining fbp1-as localizes to the cytoplasm and binds to 
polyribosomes in glucose-rich conditions. Furthermore, fbp1-as and antisense RNA 
at other stress-responsive loci are promptly degraded via the cotranslational 
nonsense-mediated decay (NMD) pathway. These results suggest NMD may potentiate 
the swift disappearance of antisense RNAs in response to cellular stress.