Identification of Novel Genes Encoding Transcription Elongation Factor TFIIS (TCEA) in Vertebrates: Conservation of Three Distinct TFIIS Isoforms in Frog, Mouse, and Human

Labhart, Paul; Morgan, Garry T.

doi:10.1006/geno.1998.5449

Cited by 39 publications

(49 citation statements)

References 29 publications

(53 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The first 80 amino acids, which are highly conserved among TFIIS proteins from different organisms, have been referred to as an ''Elongin'' domain on the basis of similar sequences within Elongin A (Aso et al 1995). The remaining 50 residues, though serine rich, vary considerably in sequence and length among organisms and have been simply termed a ''variable'' domain (Labhart and Morgan 1998).…”

Section: Resultsmentioning

confidence: 99%

“…The remaining $60 residues in the N-terminal half of TFIIS are more variable among organisms, and a chimeric gene containing human sequences in this region was unable to complement ppr2D taf14D cells ( Figure 5). This variable domain of the mouse protein has been suggested to undergo differential phosphorylation in vivo (Sekimizu et al 1981), and the observed variation in sequence and length in tissue-specific isoforms of metazoan TFIIS molecules raises the possibility of isoform-specific TFIIS functions (Umehara et al 1997;Labhart and Morgan 1998). The variable region might serve as a platform for interaction with other proteins, or it may provide a flexible tether between the four-helix bundle and the C-terminal half of TFIIS that is known to interact with RNA polymerase II (Booth et al 2000;Kettenberger et al 2003).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Genetic Interactions Between TFIIF and TFIIS

et al. 2006

View full text Add to dashboard Cite

The eukaryotic transcript elongation factor TFIIS is encoded by a nonessential gene, PPR2, in Saccharomyces cerevisiae. Disruptions of PPR2 are lethal in conjunction with a disruption in the nonessential gene TAF14/TFG3. While investigating which of the Taf14p-containing complexes may be responsible for the synthetic lethality between ppr2D and taf14D, we discovered genetic interactions between PPR2 and both TFG1 and TFG2 encoding the two larger subunits of the TFIIF complex that also contains Taf14p. Mutant alleles of tfg1 or tfg2 that render cells cold sensitive have improved growth at low temperature in the absence of TFIIS. Remarkably, the amino-terminal 130 amino acids of TFIIS, which are dispensable for the known in vitro and in vivo activities of TFIIS, are required to complement the lethality in taf14D ppr2D cells. Analyses of deletion and chimeric gene constructs of PPR2 implicate contributions by different regions of this N-terminal domain. No strong common phenotypes were identified for the ppr2D and taf14D strains, implying that the proteins are not functionally redundant. Instead, the absence of Taf14p in the cell appears to create a dependence on an undefined function of TFIIS mediated by its N-terminal region. This region of TFIIS is also at least in part responsible for the deleterious effect of TFIIS on tfg1 or tfg2 cold-sensitive cells. Together, these results suggest a physiologically relevant functional connection between TFIIS and TFIIF.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Genetic Interactions Between TFIIF and TFIIS

et al. 2006

View full text Add to dashboard Cite

show abstract

“…RNA Pol II, through stimulating the endonucleolytic cleavage of nascent RNA by RNA Pol II [65][66][67]. hPAF1 is an RNA Pol II-associated factor that facilitates transcription elongation [68].…”

Section: Monoubiquitylated Histone H2bmentioning

confidence: 99%

RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response

et al. 2011

View full text Add to dashboard Cite

a b s t r a c tThe DNA damage response (DDR) is emerging as a vast signaling network that temporarily modulates numerous aspects of cellular metabolism in the face of DNA lesions, especially critical ones such as the double strand break (DSB). The DDR involves extensive dynamics of protein post-translational modifications, most notably phosphorylation and ubiquitylation. The DSB response is mobilized primarily by the ATM protein kinase, which phosphorylates a plethora of key players in its various branches. It is based on a core of proteins dedicated to the damage response, and a cadre of proteins borrowed temporarily from other cellular processes to help meet the challenge. A recently identified novel component of the DDR pathway -histone H2B monoubiquitylationexemplifies this principle. In mammalian cells, H2B monoubiquitylation is driven primarily by an E3 ubiquitin ligase composed of the two RING finger proteins RNF20 and RNF40. Generation of monoubiquitylated histone H2B (H2Bub) has been known to be coupled to gene transcription, presumably modulating chromatin decondensation at transcribed regions. New evidence indicates that the regulatory function of H2Bub on gene expression can selectively enhance or suppress the expression of distinct subsets of genes through a mechanism involving the hPAF1 complex and the TFIIS protein. This delicate regulatory process specifically affects genes that control cell growth and genome stability, and places RNF20 and RNF40 in the realm of tumor suppressor proteins. In parallel, it was found that following DSB induction, the H2B monoubiquitylation module is recruited to damage sites where it induces local H2Bub, which in turn is required for timely recruitment of DSB repair protein and, subsequently, timely DSB repair. This pathway represents a crossroads of the DDR and chromatin organization, and is a typical example of how the DDR calls to action functional modules that in unprovoked cells regulate other processes. Ó 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. The DNA damage response: borrowing functional modules in an emergencyCellular metabolism is controlled by numerous, interlocked signaling networks. These networks are constantly responding to internal and external stimuli related to the cell's normal life cycle and functions, and to threats to its well being. A major threat to cellular homeostasis is subversion of its genomic stability, which may lead to undue cell death or to neoplasia [1,2]. DNA damage caused by internal or external damaging agents is a major danger to the integrity of the cellular genome. The cellular defense system against this threat is the DNA damage response (DDR) -an elaborate signaling network activated by DNA damage, which swiftly modulates many physiological processes [3,4]. A strong trigger of the DDR is the DNA double-strand break (DSB) [5,6]. DSBs are induced by ionizing radiation, radiomimetic chemicals, reactive oxygen species formed in the course of normal metabolism, and can also result from replic...

show abstract

“…Full-length cDNA clones encoding Xenopus TFIIS, namely po2 (Plant et al, 1996), xTFIIS.oB (Labhart and Morgan, 1998), and xTFIIS.l (Labhart, 1997), were used to create myc-tagged TFIIS constructs in two ways. In the first approach, which was used to make constructs myc-UTR-xIIS and pcxl, fragments containing the coding region and flanking untranslated regions from po2 and xTFIIS.l, respectively, were first cloned into the myc-tag vector MT-6D (Tuma et al, 1993) and then into pcDNA3 (Invitrogen Life Technologies, Paisley, UK).…”

Section: Expression Constructsmentioning

confidence: 99%

Subnuclear Localization and Cajal Body Targeting of Transcription Elongation Factor TFIIS in Amphibian Oocytes

Smith

Ling

Morgan

2003

MBoC

Self Cite

View full text Add to dashboard Cite

We have examined the localization and targeting of the RNA polymerase II (pol II) transcription elongation factor TFIIS in amphibian oocyte nuclei by immunofluorescence. Using a novel antibody against Xenopus TFIIS the major sites of immunostaining were found to be Cajal bodies, nuclear organelles that also contain pol II. Small granular structures attached to lampbrush chromosomes were also specifically stained but the transcriptionally active loops were not. Similar localization patterns were found for the newly synthesized myc-tagged TFIIS produced after injection of synthetic transcripts into the cytoplasm. The basis of the rapid and preferential targeting of TFIIS to Cajal bodies was investigated by examining the effects of deletion and site-specific mutations. Multiple regions of TFIIS contributed to efficient targeting including the domain required for its binding to pol II. The localization of TFIIS in Cajal bodies, and in particular the apparent involvement of pol II binding in achieving it, offer further support for a model in which Cajal bodies function in the preassembly of the transcriptional machinery. Although our findings are therefore consistent with TFIIS playing a role in early events of the transcription cycle, they also suggest that this elongation factor is not generally required during transcription in oocytes.

show abstract

Identification of Novel Genes Encoding Transcription Elongation Factor TFIIS (TCEA) in Vertebrates: Conservation of Three Distinct TFIIS Isoforms in Frog, Mouse, and Human

Cited by 39 publications

References 29 publications

Genetic Interactions Between TFIIF and TFIIS

Genetic Interactions Between TFIIF and TFIIS

RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response

Subnuclear Localization and Cajal Body Targeting of Transcription Elongation Factor TFIIS in Amphibian Oocytes

Contact Info

Product

Resources

About