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Alterations in the ...
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Bylund, Göran OUmeå universitet,Institutionen för medicinsk kemi och biofysik
(författare)
Alterations in the β flap and β' dock domains of the RNA polymerase abolish NusA-mediated feedback regulation of the metY-nusA-infB operon
- Artikel/kapitelEngelska2011
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LIBRIS-ID:oai:DiVA.org:umu-61270
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-61270URI
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https://doi.org/10.1128/JB.00196-11DOI
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Språk:engelska
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Sammanfattning på:engelska
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The RimM protein in Escherichia coli is important for the in vivo maturation of 30S ribosomal subunits and a ΔrimM mutant grows poorly due to assembly and translational defects. These deficiencies are suppressed partially by mutations that increase the synthesis of another assembly protein, RbfA, encoded by the metY-nusA-infB operon. Among these suppressors are mutations in nusA that impair the NusA-mediated negative-feedback regulation at internal intrinsic transcriptional terminators of the metY-nusA-infB operon. We describe here the isolation of two new mutations, one in rpoB and one in rpoC (encoding the β and β' subunits of the RNA polymerase, respectively), that increase the synthesis of RbfA by preventing NusA from stimulating termination at the internal intrinsic transcriptional terminators of the metY-nusA-infB operon. The rpoB2063 mutation changed the isoleucine in position 905 of the β flap-tip helix to a serine, while the rpoC2064 mutation duplicated positions 415 to 416 (valine-isoleucine) at the base of the β' dock domain. These findings support previously published in vitro results, which have suggested that the β flap-tip helix and β' dock domain at either side of the RNA exit tunnel mediate the binding to NusA during transcriptional pausing and termination.
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Nord, StefanUmeå universitet,Virologi(Swepub:umu)list3101
(författare)
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Lövgren, J Mattias
(författare)
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Wikström, P MikaelUmeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)(Swepub:umu)miwi0005
(författare)
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Umeå universitetInstitutionen för medicinsk kemi och biofysik
(creator_code:org_t)
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Ingår i:Journal of Bacteriology193:16, s. 4113-41220021-91931098-5530
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