Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP
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Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP. / Sheppard, Carol; Blombach, Fabian; Belsom, Adam; Schulz, Sarah; Daviter, Tina; Smollett, Katherine; Mahieu, Emilie; Erdmann, Susanne; Tinnefeld, Philip; Garrett, Roger Antony; Grohmann, Dina; Rappsilber, Juri; Werner, Finn.
I: Nature Communications, Bind 7, 13595, 2016.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP
AU - Sheppard, Carol
AU - Blombach, Fabian
AU - Belsom, Adam
AU - Schulz, Sarah
AU - Daviter, Tina
AU - Smollett, Katherine
AU - Mahieu, Emilie
AU - Erdmann, Susanne
AU - Tinnefeld, Philip
AU - Garrett, Roger Antony
AU - Grohmann, Dina
AU - Rappsilber, Juri
AU - Werner, Finn
PY - 2016
Y1 - 2016
N2 - Little is known about how archaeal viruses perturb the transcription machinery of their hosts. Here we provide the first example of an archaeo-viral transcription factor that directly targets the host RNA polymerase (RNAP) and efficiently represses its activity. ORF145 from the temperate Acidianus two-tailed virus (ATV) forms a high-affinity complex with RNAP by binding inside the DNA-binding channel where it locks the flexible RNAP clamp in one position. This counteracts the formation of transcription pre-initiation complexes in vitro and represses abortive and productive transcription initiation, as well as elongation. Both host and viral promoters are subjected to ORF145 repression. Thus, ORF145 has the properties of a global transcription repressor and its overexpression is toxic for Sulfolobus. On the basis of its properties, we have re-named ORF145 RNAP Inhibitory Protein (RIP).
AB - Little is known about how archaeal viruses perturb the transcription machinery of their hosts. Here we provide the first example of an archaeo-viral transcription factor that directly targets the host RNA polymerase (RNAP) and efficiently represses its activity. ORF145 from the temperate Acidianus two-tailed virus (ATV) forms a high-affinity complex with RNAP by binding inside the DNA-binding channel where it locks the flexible RNAP clamp in one position. This counteracts the formation of transcription pre-initiation complexes in vitro and represses abortive and productive transcription initiation, as well as elongation. Both host and viral promoters are subjected to ORF145 repression. Thus, ORF145 has the properties of a global transcription repressor and its overexpression is toxic for Sulfolobus. On the basis of its properties, we have re-named ORF145 RNAP Inhibitory Protein (RIP).
KW - Faculty of Science
KW - Archaeal biology, Enzyme mechanisms, Transcriptional regulatory elements, Virus–host interactions
U2 - 10.1038/ncomms13595
DO - 10.1038/ncomms13595
M3 - Journal article
C2 - 27882920
VL - 7
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 13595
ER -
ID: 169382662