ArticleNucleic acids research2006
A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Role of the Transcription Factor NbTFIISL in Enhancing Bamboo Mosaic Virus Accumulation via Mitochondria Localisation.Molecular plant pathology · 2025Article
- Structural basis for evolutionarily conserved interactions between TFIIS and Paf1C.International journal of biological macromolecules · 2023Article
- The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.Biochemical Society transactions · 2023Review
- Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in Saccharomyces cerevisiae.Genetics · 2022Article
- SETD2: from chromatin modifier to multipronged regulator of the genome and beyond.Cellular and molecular life sciences : CMLS · 2022Review
- The elongation factor Spn1 is a multi-functional chromatin binding protein.Nucleic acids research · 2018Article
- Biophysical Analysis of the N-Terminal Domain from the Human Protein Phosphatase 1 Nuclear Targeting Subunit PNUTS Suggests an Extended Transcription Factor TFIIS-Like Fold.The protein journal · 2016Article
- Alternative splicing of Drosophila Nmnat functions as a switch to enhance neuroprotection under stress.Nature communications · 2015Article
- Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif.Nature communications · 2015Article
- Analysis of the transgenerational iron deficiency stress memory in Arabidopsis thaliana plants.Frontiers in plant science · 2015Article
- Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.Molecular cell · 2010Article
- The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26.The EMBO journal · 2010Article
- The transcription factor Spn1 regulates gene expression via a highly conserved novel structural motif.Journal of molecular biology · 2010Article
- Arabidopsis IWS1 interacts with transcription factor BES1 and is involved in plant steroid hormone brassinosteroid regulated gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Crystallization and preliminary crystallographic analysis of eukaryotic transcription and mRNA export factor Iws1 from Encephalitozoon cuniculi.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Identification and characterization of two trypanosome TFIIS proteins exhibiting particular domain architectures and differential nuclear localizations.Molecular microbiology · 2008Article
- Comparative genomics supports a deep evolutionary origin for the large, four-module transcriptional mediator complex.Nucleic acids research · 2008Article
- Localized co-transcriptional recruitment of the multifunctional RNA-binding protein CELF1 by lampbrush chromosome transcription units.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The three structural domains of transcription elongation factor TFIIS are conserved from yeast to human. Although the N-terminal domain is not needed for transcriptional activity, a similar sequence has been identified previously in other transcription factors. We found this conserved sequence, the LW motif, in another three human proteins that are predominantly nuclear localized. We investigated two examples to determine whether the LW motif is actually a dedicated nuclear targeting signal. However, in one of the newly identified proteins, hIWS1 (human Iws1), a region containing classic nuclear localization signals (NLS) rather than the LW motif was necessary and sufficient for nuclear targeting in HeLa cells. In contrast, human TFIIS does not possess an NLS and only constructs containing the LW motif were efficiently targeted to nuclei. Moreover, mutations in the motif could cause cytoplasmic accumulation of TFIIS and enabled a structure/function assay for the domain based on the efficiency of nuclear targeting. Finally, GST pull-down assays showed that the LW motif is part of a protein-binding domain. We suggest that the targeting role the LW motif plays in TFIIS arises from its more general function as a protein interaction domain, enabling TFIIS to bind a carrier protein(s) that accomplishes nuclear import.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.