Ej. Steinmetz et al., RNA-binding protein Nrd1 directs poly(A)-independent 3 '-end formation of RNA polymerase II transcripts, NATURE, 413(6853), 2001, pp. 327-331
A eukaryotic chromosome contains many genes, each transcribed separately by
RNA polymerase (pol) I, II or III. Transcription termination between genes
prevents the formation of polycistronic RNAs and anti-sense RNAs, which ar
e generally detrimental to the correct expression of genes. Terminating the
transcription of protein-coding genes by pol II requires a group of protei
ns that also direct cleavage and polyadenylation of the messenger RNA in re
sponse to a specific sequence element, and are associated with the carboxyl
-terminal domain of the largest subunit of pol II (refs 1-6). By contrast,
the cis-acting elements and trans-acting factors that direct termination of
non-polyadenylated transcripts made by pol II, including small nucleolar a
nd small nuclear RNAs, are not known. Here we show that read-through transc
ription from yeast small nucleolar RNA and small nuclear RNA genes into adj
acent genes is prevented by a cis-acting element that is recognized, in par
t, by the essential RNA-binding protein Nrd1. The RNA-binding protein Nab3,
the putative RNA helicase Sen1, and the intact C-terminal domain of pol II
are also required for efficient response to the element. The same proteins
are required for maintaining normal levels of Nrd1 mRNA, indicating that t
hese proteins may control elongation of a subset of mRNA transcripts.