ArticleMolecular and cellular biology1999
The SKN-1 amino-terminal arm is a DNA specificity segment.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Coordinated control of proteasome subunit gene expression promotes stress resistance, proteostasis, and longevity.GeroScience · 2026Article
- Model organisms for investigating the functional involvement of NRF2 in non-communicable diseases.Redox biology · 2025Review
- Disrupting the SKN-1 homeostat: mechanistic insights and phenotypic outcomes.Frontiers in aging · 2024Review
- Decomposing protein-DNA binding and recognition using simplified protein models.Nucleic acids research · 2017Article
- How proteins bind to DNA: target discrimination and dynamic sequence search by the telomeric protein TRF1.Nucleic acids research · 2017Article
- Conservation of the Keap1-Nrf2 System: An Evolutionary Journey through Stressful Space and Time.Molecules (Basel, Switzerland) · 2017Review
- Dynamics and recognition within a protein-DNA complex: a molecular dynamics study of the SKN-1/DNA interaction.Nucleic acids research · 2016Article
- SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans.Free radical biology & medicine · 2015Review
- Unique structure and regulation of the nematode detoxification gene regulator, SKN-1: implications to understanding and controlling drug resistance.Drug metabolism reviews · 2012Review
- Condition-adapted stress and longevity gene regulation by Caenorhabditis elegans SKN-1/Nrf.Aging cell · 2009Article
- SKN-1 links C. elegans mesendodermal specification to a conserved oxidative stress response.Genes & development · 2003Article
- Regulation of cyclic peptide biosynthesis in a plant pathogenic fungus by a novel transcription factor.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- DNA sequence-dependent folding determines the divergence in binding specificities between Maf and other bZIP proteins.The EMBO journal · 2001Article
- Establishment of distinct MyoD, E2A, and twist DNA binding specificities by different basic region-DNA conformations.Molecular and cellular biology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Caenorhabditis elegans SKN-1 protein binds DNA through a basic region like those of bZIP proteins and through a flexible amino-terminal arm segment similar to those with which numerous helix-turn-helix proteins bind to bases in the minor groove. A recent X-ray crystallographic structure suggests that the SKN-1 amino-terminal arm provides only nonspecific DNA binding. In this study, however, we demonstrate that this segment mediates recognition of an AT-rich element that is part of the preferred SKN-1 binding site and thereby significantly increases the sequence specificity with which SKN-1 binds DNA. Mutagenesis experiments show that multiple amino acid residues within the arm are involved in binding. These residues provide binding affinity through distinct but partially redundant interactions and enhance specificity by discriminating against alternate sites. The AT-rich element minor groove is important for binding of the arm, which appears to affect DNA conformation in this region. This conformational effect does not seem to involve DNA bending, however, because the arm does not appear to affect a modest DNA bend that is induced by SKN-1. The data illustrate an example of how a small, flexible protein segment can make an important contribution to DNA binding specificity through multiple interactions and mechanisms.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.