Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
Author
dc.contributor.author
Yue, Zhenyu
Author
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Maldonado, Edio
Author
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Pillutla, Renuka
Author
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Cho, Helen
Author
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Reinberg, Danny
Author
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Shatkin, Aaron J.
Admission date
dc.date.accessioned
2019-01-29T15:54:53Z
Available date
dc.date.available
2019-01-29T15:54:53Z
Publication date
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1997
Cita de ítem
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Proceedings of the National Academy of Sciences of the United States of America, Volumen 94, Issue 24, 2018, Pages 12898-12903
Identifier
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00278424
Identifier
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10.1073/pnas.94.24.12898
Identifier
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https://repositorio.uchile.cl/handle/2250/162727
Abstract
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5'-Capping is an early mRNA modification that has important consequences for downstream events in gene expression. We have isolated mammalian cDNAs encoding capping enzyme. They contain the sequence motifs characteristic of the nucleotidyl transferase superfamily. The predicted mouse and human enzymes consist of 597 amino acids and are 95% identical. Mouse cDNA directed synthesis of a guanylylated 68-kDa polypeptide that also contained RNA 5'- triphosphatase activity and catalyzed formation of RNA 5'-terminal GpppG. A haploid strain of Saccharomyces cerevisiae lacking mRNA guanylyltransferase was complemented for growth by the mouse cDNA. Conversion of Lys-294 in the KXDG-conserved motif eliminated both guanylylation and complementation, identifying it as the active site. The K294A mutant retained RNA 5'- triphosphatase activity, which was eliminated by N-terminal truncation. Full- length capping enzyme and an active C-terminal fragment bound to the elongating form and not to the initi
Proceedings of the National Academy of Sciences of the United States of America
Keywords
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Multidisciplinary
Título
dc.title
Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II