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An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch.


ABSTRACT: Antitermination protein N regulates the transcriptional program of phage lambda through recognition of RNA enhancer elements. Binding of an arginine-rich peptide to one face of an RNA hairpin organizes the other, which in turn binds to the host antitermination complex. The induced RNA structure mimics a GNRA hairpin, an organizational element of rRNA and ribozymes. The two faces of the RNA, bridged by a sheared GA base pair, exhibit a specific pattern of base stacking and base flipping. This pattern is extended by stacking of an aromatic amino acid side chain with an unpaired adenine at the N-binding surface. Such extended stacking is coupled to induction of a specific internal RNA architecture and is blocked by RNA mutations associated in vivo with loss of transcriptional antitermination activity. Mimicry of a motif of RNA assembly by an RNA-protein complex permits its engagement within the antitermination machinery.

SUBMITTER: Su L 

PROVIDER: S-EPMC275392 | biostudies-literature | 1997 Sep

REPOSITORIES: biostudies-literature

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An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch.

Su L L   Radek J T JT   Labeots L A LA   Hallenga K K   Hermanto P P   Chen H H   Nakagawa S S   Zhao M M   Kates S S   Weiss M A MA  

Genes & development 19970901 17


Antitermination protein N regulates the transcriptional program of phage lambda through recognition of RNA enhancer elements. Binding of an arginine-rich peptide to one face of an RNA hairpin organizes the other, which in turn binds to the host antitermination complex. The induced RNA structure mimics a GNRA hairpin, an organizational element of rRNA and ribozymes. The two faces of the RNA, bridged by a sheared GA base pair, exhibit a specific pattern of base stacking and base flipping. This pat  ...[more]

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