2007
DOI: 10.1016/j.bbrc.2007.01.119
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Crystal structure and RNA-binding analysis of the archaeal transcription factor NusA

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Cited by 17 publications
(17 citation statements)
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References 30 publications
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“…The transcriptional regulation-related proteins corresponded to a putative transcription regulator (spot 32) and the transcription factor NusA (spot 33) involved in the intrinsic termination of transcription [57]. NusA has been also reported to display important functions in the cellular response to adverse factors [58].…”
Section: Resultsmentioning
confidence: 99%
“…The transcriptional regulation-related proteins corresponded to a putative transcription regulator (spot 32) and the transcription factor NusA (spot 33) involved in the intrinsic termination of transcription [57]. NusA has been also reported to display important functions in the cellular response to adverse factors [58].…”
Section: Resultsmentioning
confidence: 99%
“…Archaeal genomes do not encode Rho‐like factors and archaeal NusA lacks the N‐terminal RNAP interaction domain. However, the two KH domains are highly conserved and it has recently been shown that the archaeal Aeropyrum pernix NusA binds to transcript sequences located at the 3′ terminus of rRNA with high affinity ( K d ∼60 nM; Shibata et al ., 2007). Transcription termination in the archaea is mediated by T‐rich sequences at the 3′ end of genes but appears to be independent of specific RNA secondary structures (Santangelo and Reeve, 2006).…”
Section: Post‐initiation Regulation Of Transcriptionmentioning
confidence: 99%
“…Archaeal genomes do not encode Rho-like factors and archaeal NusA lacks the N-terminal RNAP interaction domain. However, the two KH domains are highly conserved and it has recently been shown that the archaeal Aeropyrum pernix NusA binds to transcript sequences located at the 3′ terminus of rRNA with high affinity (K d~60 nM; Shibata et al, 2007).…”
Section: Post-initiation Regulation Of Transcriptionmentioning
confidence: 99%
“…These stems presumably maintain the looped conformation to provide time for rRNA folding to complete before processing by dedicated RNases (12). The association of the KH domain with rRNA biogenesis is consistent with its distribution pattern: Archaea, but not eukaryotes, harbor a factor that displays high sequence identity to KH-KH repeats of bacterial NusA and similar spacerless head-to-tail packing (116). Intriguingly, the presumed loss of KH domains in eukaryotes coincides with the evolution of a specialized RNAP for rRNA synthesis and, perhaps more importantly, a principally different rRNA folding mechanism (124).…”
Section: Nus Factors and Rrna Antitermination Complexesmentioning
confidence: 62%