ArticleNucleic acids research2015
DNA-binding proteins from marine bacteria expand the known sequence diversity of TALE-like repeats.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Prevalence and diversity of TAL effector-like proteins in fungal endosymbioticMicrobial genomics · 2024Article
- TALE-induced cell death executors: an origin outside immunity?Trends in plant science · 2022Review
- TALEs as double-edged swords in plant-pathogen interactions: Progress, challenges, and perspectives.Plant communications · 2022Review
- Review
- A TAL effector-like protein of an endofungal bacterium increases the stress tolerance and alters the transcriptome of the host.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Tal1Frontiers in microbiology · 2019Article
- Engineering altered protein-DNA recognition specificity.Nucleic acids research · 2018Review
- Exploiting the sequence diversity of TALE-like repeats to vary the strength of dTALE-promoter interactions.Synthetic biology (Oxford, England) · 2017Article
- A TALE-inspired computational screen for proteins that contain approximate tandem repeats.PloS one · 2017Article
- A Conserved Basal Transcription Factor Is Required for the Function of Diverse TAL Effectors in Multiple Plant Hosts.Frontiers in plant science · 2017Article
- Article
- TALE-Like Effectors Are an Ancestral Feature of the Ralstonia solanacearum Species Complex and Converge in DNA Targeting Specificity.Frontiers in plant science · 2016Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription Activator-Like Effectors (TALEs) of Xanthomonas bacteria are programmable DNA binding proteins with unprecedented target specificity. Comparative studies into TALE repeat structure and function are hindered by the limited sequence variation among TALE repeats. More sequence-diverse TALE-like proteins are known from Ralstonia solanacearum (RipTALs) and Burkholderia rhizoxinica (Bats), but RipTAL and Bat repeats are conserved with those of TALEs around the DNA-binding residue. We study two novel marine-organism TALE-like proteins (MOrTL1 and MOrTL2), the first to date of non-terrestrial origin. We have assessed their DNA-binding properties and modelled repeat structures. We found that repeats from these proteins mediate sequence specific DNA binding conforming to the TALE code, despite low sequence similarity to TALE repeats, and with novel residues around the BSR. However, MOrTL1 repeats show greater sequence discriminating power than MOrTL2 repeats. Sequence alignments show that there are only three residues conserved between repeats of all TALE-like proteins including the two new additions. This conserved motif could prove useful as an identifier for future TALE-likes. Additionally, comparing MOrTL repeats with those of other TALE-likes suggests a common evolutionary origin for the TALEs, RipTALs and Bats.
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