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Interaction of a nascent RNA structure with RNA polymerase is required for hairpin-dependent transcriptional pausing but not for transcript release

Article Abstract:

Nascent RNA structures may exert control over elongation or RNA chains directly by interacting with RNA polymerase or in an indirect way by disrupting RNA contacts at the nascent stage with DNA or polymerase. Effects of the his (ital) leader pause RNA hairpin have been tested for ability to be mimicked by pairing of antisense DNA or RNA oligonucleotides to the nascent transcript. It was shown that a nascent RNA structure must interact with RNA polymerase for hairpin-dependent transcriptional pausing. It is not necesary for transcript release.

Author: Landick, Robert, Artsimovitch, Irina
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Observations, Antisense RNA, Cellular signal transduction, Genetic regulation, Genetic transcription, Transcription (Genetics), RNA polymerases, Cellular control mechanisms, Cell regulation, Nucleic acids, Nucleic acid isolation

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ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motif

Article Abstract:

Herpes simplex virus 1 (HSV-1) has an essential regulatory protein ICP27. It works against host cell-slicing so that unspiced transcripts accumulate in the nucleus. It also helps in RNA export of viral intronless mRNAs. ICP27 shuttles back and forth between the nucleus and cytoplasm through a nuclear export signal with much leucine. ICP27 can be crosslinked to poly(A)+ RNA in cytoplasm and in a nucleus to support a role in export. An arginine-glycine region very like an RGG box is required for the binding of ICP27 to RNA in vivo.

Author: Sandri-Goldin, Rozanne M.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Research, Gene expression, Herpes simplex virus, Viral genetics

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Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes

Article Abstract:

A study observed the substrates on which proteins act and the functions of assembly factors which were previously unknown. Results revealed that Rpf2 and Rrs1 were required for recruiting rpL5, rpL11and 5S ribosomal RNA into ribosomes.

Author: Jakovljevic, Jelena, Oeffinger, Marlene, Hiley, Shawna L., Rout, Michael P., Harnpicharnchai, Piyanun, Lan Tang, Guo, Yurong, Hughes, Timothy, Woolford, John L., Jr.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2007
Physiological aspects, Eukaryotes, Ribosomal proteins, Properties, RNA synthesis

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Subjects list: Analysis, Genetic aspects, RNA
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