DNA-binding proteins from marine bacteria expand the known sequence diversity of TALE-like repeats

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 TAL...

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Bibliographic Details
Published in:Nucleic acids research 2015-11, Vol.43 (20), p.10065-10080
Main Authors: de Lange, Orlando, Wolf, Christina, Thiel, Philipp, Krüger, Jens, Kleusch, Christian, Kohlbacher, Oliver, Lahaye, Thomas
Format: Article
Language:English
Subjects:
Aquatic Organisms
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
DNA - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Genetic Variation
Metagenomics
Protein Binding
Protein Stability
Recombinant Fusion Proteins - metabolism
Repetitive Sequences, Amino Acid
Structural Homology, Protein
Synthetic Biology and Bioengineering
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Summary: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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkv1053