An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in
            <i>Saccharomyces cerevisiae</i>

Archambault, Jacques; Chambers, Ross; Kobor, Michæl S.; Ho, Yuen; Cartier, Mireille; Bolotin, Diana; Andrews, Brenda; Kane, Caroline M.; Greenblatt, Jack

doi:10.1073/pnas.94.26.14300

Cited by 137 publications

(195 citation statements)

References 57 publications

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“…TFIIF stimulates activity of FCP1, the pol II CTD phosphatase purified from human cells (22). Partial cDNAs encoding the human enzyme were originally identified in a yeast two-hybrid screen as RAP74-interacting proteins (23). The results of domain mapping of interactions between FCP1 and RAP74 are consistent with direct binding of the C-terminal region of FCP1 (760-842) to the C-terminal region of RAP74 (436-517) (23).…”

Section: Resultsmentioning

confidence: 82%

“…The activity of this HeLa cell CTD phosphatase is stimulated by the RAP74 subunit of TFIIF, and this stimulation can be inhibited by TFIIB (22). A yeast two-hybrid screen for RAP74-interacting proteins produced partial cDNAs encoding a human CTD phosphatase, FCP1 (23,24). The C-terminal region (residues 436-517) of human RAP74, which interacts with the FCP1 phosphatase, is both necessary and sufficient for RAP74-mediated stimulation of CTD phosphatase activity in vitro (23).…”

mentioning

confidence: 99%

“…A yeast two-hybrid screen for RAP74-interacting proteins produced partial cDNAs encoding a human CTD phosphatase, FCP1 (23,24). The C-terminal region (residues 436-517) of human RAP74, which interacts with the FCP1 phosphatase, is both necessary and sufficient for RAP74-mediated stimulation of CTD phosphatase activity in vitro (23). TFIIF modulation of FCP1 activity underscores the importance of the pol II phosphorylation cycle in the transcription initiation and elongation reactions.…”

mentioning

confidence: 99%

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Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

Kamada

Angelis

Roeder

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-Å resolution. The ␣͞␤ structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3␥ (HNF-3␥), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3␥ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the ␤ subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 wingedhelix domain.T ranscription of class II nuclear genes in eukaryotes requires a complex assembly of proteins composed of a multisubunit RNA polymerase II (pol II) and general transcription factors (TFIIs), which are required for assembly of the preinitiation complex (PIC) on promoter DNA and initiation of transcription (1). In the most general case, PIC assembly begins with the TATA box-binding protein (TBP) subunit of TFIID recognizing the TATA element, followed by coordinated accretion of TFIIB, the nonphosphorylated form of pol II plus TFIIF, TFIIE, and TFIIH. Transcription initiation is followed by phosphorylation of the C-terminal domain (CTD) of the largest subunit of pol II, which in turn facilitates promoter clearance and productive elongation. After elongation and termination of pre-mRNA synthesis, a phosphatase recycles pol II to its nonphosphorylated form, allowing the enzyme and the requisite TFIIs to initiate the next round of transcription.Mammalian TFIIF is an ␣␤ hetero-oligomer of RAP74 and RAP30 subunits (RNA polymerase II-associating proteins; 58 kDa and 28 kDa, respectively) (2), which binds to pol II in solution and facilitates delivery of the polymerase to the TFIID-TFIIB-DNA complex on the promoter. TFIIF was originally identified on the basis of physical association with pol II, and its requirement for promoter-specific transcription initiation by this large multisubunit enzyme. Within the PIC, TFIIF stabilizes binding of pol II to TFIID and TFIIB at the promoter (3-5). Moreover, TFIIF is required for entry of TFIIE and TFIIH into the PIC, for subsequent open complex formation catalyzed by the DNA helicase subunit of TFIIH (5-7), and for synthesis of the first phosphodiester bond of nascent transcripts (8-10). It is also possible that TFIIF acts as a scaffold for binding of TFIIH to the growing PIC and͞or that TFIIF actively participates in formation of the open complex. Photocrosslinking experiments suggest that TFIIF interacts with promoter DNA to induce a dramatic conformational change that results in wrapping of DNA around pol II and the class II general transcription factors within the PIC (11-14).Biochemical properties of TFIIF have been attributed to distinct polypeptide chain segments of each of subunit. Mammalian RAP30 can b...

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Section: Resultsmentioning

confidence: 82%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

Kamada

Angelis

Roeder

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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“…It has been purified from yeast and mammalian cells (8,9), and the corresponding cDNA has been cloned by a two-hybrid screen using the RAP74 subunit of the general transcription factor TFIIF as a bait (10). FCP1 (TFIIF-dependent CTD Phosphatase 1) consists of a single 150-kDa polypeptide subunit (11,12).…”

Section: Rna Polymerase II (Rnap Ii)mentioning

confidence: 99%

“…CK2 Phosphorylation Enhances the Binding of FCP1 to the RAP74 Subunit of TFIIF-Genuine FCP1 is known to bind strongly to the RAP74 subunit of TFIIF, and this interaction stimulates phosphatase activity (10,15,16). To investigate a possible modulation of FCP1 binding to TFIIF by phosphorylation, a Far Western blot was performed using recombinant xRAP74 as a probe.…”

Section: Ck2 Is the Major Fcp1 Kinase Present In Eggmentioning

confidence: 99%

FCP1 Phosphorylation by Casein Kinase 2 Enhances Binding to TFIIF and RNA Polymerase II Carboxyl-terminal Domain Phosphatase Activity

Palancade

Dubois

Bensaude

2002

Journal of Biological Chemistry

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Dephosphorylation of RNA polymerase II carboxylterminal domain (CTD) is required to resume sequential transcription cycles. FCP1 (TFIIF-dependent CTD phosphatase 1) is the only known phosphatase targeting RNAP II CTD. Here we show that in Xenopus laevis cells, xFCP1 is a phosphoprotein. On the basis of biochemical fractionation and drug sensitivity, casein kinase 2 (CK2) is shown to be the major kinase involved in xFCP1 phosphorylation in X. laevis egg extracts. CK2 phosphorylates xFCP1 mainly at a cluster of serines centered on Ser 457 . CK2-dependent phosphorylation enhances 4-fold the CTD phosphatase activity of FCP1 and its binding to the RAP74 subunit of general transcription factor TFIIF. These findings unravel a new mechanism regulating CTD phosphorylation and hence class II gene transcription.RNA polymerase II (RNAP II) 1 is a multiprotein complex in charge of eucaryotic mRNA synthesis (1). Rpb1, the largest RNAP II subunit, is extensively phosphorylatable on its carboxyl-terminal domain (CTD), which consists of up to 52 repeats of the consensus heptapeptide Tyr-Ser-Pro-Thr-Ser-ProSer (2). Two phosphoisoforms of RNAP II coexist in somatic cells in a dynamic equilibrium (3). The hypophosphorylated IIA form assembles into preinitiation complexes, whereas the hyperphosphorylated IIO form elongates mRNA synthesis and recruits mRNA processing factors (4). The conversion from IIA to IIO occurs during initiation and elongation of transcription and involves CTD kinases such as CDK7 and CDK9, respectively, included in the transcription factors TFIIH and p-TEFb (5, 6). CTD dephosphorylation is required to recycle RNAP II after a transcriptional round (7).In contrast to the numerous CTD kinases identified, only one CTD phosphatase has been characterized so far. It has been purified from yeast and mammalian cells (8,9), and the corresponding cDNA has been cloned by a two-hybrid screen using the RAP74 subunit of the general transcription factor TFIIF as a bait (10). FCP1 (TFIIF-dependent CTD Phosphatase 1) consists of a single 150-kDa polypeptide subunit (11, 12). FCP1does not display any homology with other known protein phosphatases but possesses an unusual catalytic site present in a subset of phosphotransferases (13,14). FCP1 is a highly specific phosphatase as the CTD within a functional RNAP II remains its only known protein substrate. FCP1 is recruited to RNAP II through docking sites on the Rpb4 subunit of RNAP II and on the RAP74 subunit of TFIIF (15, 16).FCP1 activity is regulated at various levels. First, competitive binding of general transcription factors TFIIF and TFIIB to FCP1 carboxyl-terminal domain, respectively, stimulates or inhibits its phosphatase activity (15,17). Second, free RNAP IIO molecules are better substrates than molecules engaged in transcription elongation complexes (18,19). Third, inhibition of FCP1 phosphatase activity by the human immunodeficiency viral protein Tat may contribute to stimulate transcriptional elongation from the human immunodeficiency virus promoter (20, 21).We had...

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Identification of a protein that interacts with the golli‐myelin basic protein and with nuclear LIM interactor in the nervous system

Fernandes

Campagnoni

Kampf

et al. 2003

J of Neuroscience Research

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The myelin basic protein (MBP) gene encodes the classic MBPs and the golli proteins, which are related structurally to the MBPs but are not components of the myelin sheath. A yeast two-hybrid approach was used to identify molecular partners that interact with the golli proteins. A mouse cDNA was cloned that encoded a protein of 261 amino acids and called golli-interacting protein (GIP). Database analysis revealed that GIP was the murine homolog of human nuclear LIM interactor-interacting factor (NLI-IF), a nuclear protein whose function is just beginning to be understood. It is a member of a broad family of molecules, found in species ranging from yeast to human, that contain a common domain of approximately 100 amino acids. Immunocytochemical and Northern blot analyses showed co-expression of GIP and golli in several neural cell lines. GIP and golli also showed a similar developmental pattern of mRNA expression in brain, and immunohistochemical staining of GIP and golli showed co-expression in several neuronal populations and in oligodendrocytes in the mouse brain. GIP was localized predominantly in nuclei. GIP co-immunoprecipitated with golli in several in vitro assays as well as from PC12 cells under physiologic conditions. GIP was the first member of this family shown to interact with nuclear LIM interactor (NLI). NLI co-immunoprecipitated with GIP and golli from lysates of N19 cells transfected with NLI, further confirming an interaction between golli, GIP, and NLI. The ability of GIP to interact with both golli and NLI, and the nuclear co-localization of GIP and golli in many cells, indicates a role for the golli products of the MBP gene in NLI- associated regulation of gene expression.

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An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae

Cited by 137 publications

References 57 publications

Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

FCP1 Phosphorylation by Casein Kinase 2 Enhances Binding to TFIIF and RNA Polymerase II Carboxyl-terminal Domain Phosphatase Activity

Identification of a protein that interacts with the golli‐myelin basic protein and with nuclear LIM interactor in the nervous system

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