Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP

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 - 2016/11/24

Y1 - 2016/11/24

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

SN - 2041-1723

VL - 7

JO - Nature Communications

JF - Nature Communications

M1 - 13595

ER -