A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus (Q27929520)

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English	A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus	scientific article

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scholarly article

1 reference

30 November 2016

A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus (English)

1 reference

30 November 2016

Polynucleotide 5'-phosphatase YPL228W

1 reference

GOA release 2020-03-11

MRNA guanylyltransferase YGL130W

1 reference

GOA release 2020-03-11

author name string

S Shuman

5

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K Lehman

1

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I Rouzankina

4

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C K Ho

3

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B Schwer

2

0 references

language of work or name

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publication date

6 August 1999

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Journal of Biological Chemistry

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30 November 2016

274

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22668-78

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32

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Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5'-triphosphatase, which is essential for cell viability

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

5'-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Isolation and characterization of the Candida albicans gene for mRNA 5'-triphosphatase: association of mRNA 5'-triphosphatase and mRNA 5'-guanylyltransferase activities is essential for the function of mRNA 5'-capping enzyme in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Phylogenetic relationships of fungal cytochromes c.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Distinct roles for CTD Ser-2 and Ser-5 phosphorylation in the recruitment and allosteric activation of mammalian mRNA capping enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Mutational analysis of yeast mRNA capping enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Domain structure of vaccinia DNA ligase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Yeast and viral RNA 5' triphosphatases comprise a new nucleoside triphosphatase family

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22668

21 January 2018

Identifiers

10.1074/JBC.274.32.22668

0 references

1 reference

30 November 2016

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