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Volumn 10, Issue 3, 1998, Pages 323-331

The cellular organization of gene expression

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA PRECURSOR;

EID: 0031834613     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80007-0     Document Type: Article
Times cited : (207)

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    • of outstanding interest. The carboxy-terminal domain of RNA polymerase II was used as bait in a yeast two-hybrid screen and four novel SR-domain-containing proteins were identified which specifically bind to the carboxyl-terminal domain of RNA polymerase II.
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    • of outstanding interest. The hyperphosphorylated form of the large subunit of RNA polymerase II co-immunoprecipitated with splicing factors. This association was shown to be maintained in the absence of pre-mRNA and did not require the polymerase to be transcriptionally engaged.
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    • of outstanding interest. The function of the carboxy-terminal domain (CTD) was analyzed in vivo using mutants of the large subunit of RNA polymerase II lacking the CTD. 3′ cleavage factors failed to associate with the form of the large subunit lacking the CTD and both pre-mRNA splicing and 3′ cleavage was blocked in the absence of the CTD.
    • McCracken S, Fong N, Yankulov K, Ballantyne S, Pan G, Greenblatt J, Patterson SD, Wickens M, Bentley DL. The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. of outstanding interest Nature. 385:1997;357-361 The function of the carboxy-terminal domain (CTD) was analyzed in vivo using mutants of the large subunit of RNA polymerase II lacking the CTD. 3′ cleavage factors failed to associate with the form of the large subunit lacking the CTD and both pre-mRNA splicing and 3′ cleavage was blocked in the absence of the CTD.
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    • Amgen EST Program. of outstanding interest. 5′ capping enzymes were found to bind specifically to the phosphorylated form of the carboxy-terminal domain of RNA polymerase II and truncation of the domain resulted in a reduction of mRNA capping in vivo. These findings suggest that the carboxy-terminal domain coordinates 5′ capping with transcription.
    • Amgen EST Program McCracken S, Feng N, Rosonina E, Yankulov K, Brothers G, Siderovski D, Hessel A, Foster S, Shuman S, Bentley D. 5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. of outstanding interest Genes Dev. 11:1997;3306-3318 5′ capping enzymes were found to bind specifically to the phosphorylated form of the carboxy-terminal domain of RNA polymerase II and truncation of the domain resulted in a reduction of mRNA capping in vivo. These findings suggest that the carboxy-terminal domain coordinates 5′ capping with transcription.
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    • of outstanding interest. Enzymes that catalyze 5′ capping were found to bind specifically to the phosphorylated form of the carboxy-terminal domain of RNA polymerase II. Conditional mutations of this domain were found to be lethal when combined with a capping enzyme mutation.
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    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • of outstanding interest. Enzymes that catalyze 5′ capping were found to bind specifically to the elongating but not initiating form of RNA polymerase II.
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