GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:8692929

From GONUTS
Jump to: navigation, search
Citation

Yuryev, A, Patturajan, M, Litingtung, Y, Joshi, RV, Gentile, C, Gebara, M and Corden, JL (1996) The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins. Proc. Natl. Acad. Sci. U.S.A. 93:6975-80

Abstract

Although transcription and pre-mRNA processing are colocalized in eukaryotic nuclei, molecules linking these processes have not previously been described. We have identified four novel rat proteins by their ability to interact with the repetitive C-terminal domain (CTD) of RNA polymerase II in a yeast two-hybrid assay. A yeast homolog of one of the rat proteins has also been shown to interact with the CTD. These CTD-binding proteins are all similar to the SR (serine/arginine-rich) family of proteins that have been shown to be involved in constitutive and regulated splicing. In addition to alternating Ser-Arg domains, these proteins each contain discrete N-terminal or C-terminal CTD-binding domains. We have identified SR-related proteins in a complex that can be immunoprecipitated from nuclear extracts with antibodies directed against RNA polymerase II. In addition, in vitro splicing is inhibited either by an antibody directed against the CTD or by wild-type but not mutant CTD peptides. Thus, these results suggest that the CTD and a set of CTD-binding proteins may act to physically and functionally link transcription and pre-mRNA processing.

Links

PubMed PMC38919

Keywords

Amino Acid Sequence; Animals; Arginine; Binding Sites; Carrier Proteins/biosynthesis; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Consensus Sequence; Macromolecular Substances; Mice; Molecular Sequence Data; RNA Polymerase II/chemistry; RNA Polymerase II/metabolism; RNA-Binding Proteins/chemistry; Rats; Recombinant Fusion Proteins/metabolism; Saccharomyces cerevisiae/metabolism; Sequence Homology, Amino Acid; Serine

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:RPB1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q63625

F

Seeded From UniProt

complete

RAT:SCAF8

enables

GO:0019904: protein domain specific binding

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

RAT:SCAF8

involved_in

GO:0006397: mRNA processing

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:SCAF8

involved_in

GO:0006366: transcription by RNA polymerase II

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:SFR19

enables

GO:0019904: protein domain specific binding

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

RAT:SFR19

involved_in

GO:0006397: mRNA processing

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:SFR19

involved_in

GO:0006366: transcription by RNA polymerase II

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:PHRF1

enables

GO:0019904: protein domain specific binding

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

RAT:PHRF1

involved_in

GO:0006397: mRNA processing

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:PHRF1

involved_in

GO:0006366: transcription by RNA polymerase II

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

RAT:PHRF1

enables

GO:0070063: RNA polymerase binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P08775

F

Seeded From UniProt

complete

RAT:SCAF4

enables

GO:0008022: protein C-terminus binding

ECO:0000353: physical interaction evidence used in manual assertion

RGD:1557071

F

Seeded From UniProt

complete

RAT:SCAF4

involved_in

GO:0006397: mRNA processing

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

See Help:References for how to manage references in GONUTS.