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Significance We directly visualize cotranslocation on DNA by the alkyltransferase-like protein, ATL, and UvrA, the initiating enzyme of prokaryotic nucleotide excision repair (NER). Our findings offer an enhanced understanding of the recruitment of NER to nonnative NER target lesions. Furthermore, we elucidate the mechanism of DNA lesion search and recognition by ATL and its catalytically active homolog AGT. Our data support a paradigm for the transition from oligomeric lesion search complexes of ATL (and AGT) to the repair-initiating, monomeric protein complexes based on the dissociation of oligomeric structures due to stable, stronger DNA bending at a target lesion.

Alkyltransferase-like protein clusters scan DNA rapidly over long distances and recruit NER to alkyl-DNA lesions