ArticleCellular and molecular life sciences : CMLS2014
A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor.
Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- A noncanonical transcriptional regulation in natural product biosynthesis.Nucleic acids research · 2026Article
- Functional connexion of bacterioferritin in antibiotic production and morphological differentiation in Streptomyces coelicolor.Microbial cell factories · 2024Article
- Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein.Journal of bacteriology · 2022Review
- Structural Insights into Iron Ions Accumulation in Dps Nanocage.International journal of molecular sciences · 2022Article
- Identification of FtpA, a Dps-Like Protein Involved in Anti-Oxidative Stress and Virulence in Actinobacillus pleuropneumoniae.Journal of bacteriology · 2022Article
- Dps-DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration.European biophysics journal : EBJ · 2021Article
- Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.FEBS open bio · 2020Article
- A highly processive actinobacterial topoisomerase I - thoughts onMicrobiology (Reading, England) · 2020Review
- Unreported intrinsic disorder in proteins: Disorder emergency room.Intrinsically disordered proteins · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Dps proteins are members of an extensive family of proteins that oxidise and deposit iron in the form of ferric oxide, and are also able to bind DNA. Ferroxidation centres are formed at the interface of anti-parallel dimers, which further assemble into dodecameric nanocages with a hollow core where ferric oxide is deposited. Streptomyces coelicolor encodes three Dps-like proteins (DpsA, B and C). Despite sharing the conserved four-helix bundle organisation observed in members of the Dps family, they display significant differences in the length of terminal extensions, or tails. DpsA possess both N- and C-terminal tails of different lengths, and their removal affects quaternary structure assembly to varying degrees. DpsC quaternary structure, on the other hand, is heavily dependent on its N-terminal tail as its removal abolishes correct protein folding. Analysis of the crystal structure of dodecamers from both proteins revealed remarkable differences in the position of tails and interface surface area; and provides insight to explain the differences in biochemical behaviour observed while comparing DpsA and DpsC.
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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.